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1. The structural features of an ancient ribonuclease from Salmo salar reveal an intriguing case of auto-inhibition

Author: Rosanna Culurciello, Mariateresa Trapani, Irene Russo Krauss, Elio Pizzo, Carla Carluccio, Andrea Bosso, Antonello Merlino, Lelio Mazzarella, Filomena Sica, Romualdo Troisi, Sica, F., Russo Krauss, I., Troisi, R., Bosso, A., Culurciello, R., Carluccio, C., Trapani, M., Merlino, A., Mazzarella, L., and Pizzo, E.
Subjects: Fish Proteins, Protein Folding, Evolution, Protein Domain, RNase P, Salmo salar, Mutant, 02 engineering and technology, Biochemistry, Pentapeptide repeat, Ribonuclease, Evolution, Molecular, 03 medical and health sciences, Ribonucleases, Auto-inhibition, Protein Domains, Structural Biology, Catalytic triad, Animals, Molecular Biology, Histidine, 030304 developmental biology, 0303 health sciences, biology, Animal, Chemistry, Crystal structure, Active site, General Medicine, 021001 nanoscience & nanotechnology, Cell biology, Folding (chemistry), Fish Protein, biology.protein, 0210 nano-technology
Abstract: The superfamily of vertebrate ribonucleases, a large group of evolutionarily related proteins, continues to provide interesting structural and functional information. In particular, the crystal structure of SS-RNase-2 from Salmo salar (SS2), here presented, has revealed a novel auto-inhibition mechanism that enriches the number of inhibition strategies observed in some members of the family. Within an essentially unmodified RNase folding, the SS2 active site cleft is in part obstructed by the collapse of an extra pentapeptide inserted in the C-terminal region. This unexpected intrusion alters the organization of the catalytic triad by pushing one catalytic histidine off the pocket. Possible mechanisms to remove the active site obstruction have also been studied through the production of two mutants that provide useful information on the functionality of this intriguing version of the ribonuclease superfamily.
Published: 2021
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2. Molecular recognition of sialoglycans by streptococcal Siglec-like adhesins: toward the shape of specific inhibitors

Author: Cristina Di Carluccio, Alba Silipo, Yoshiyuki Manabe, Roberta Marchetti, Marco Fragai, Elio Pizzo, Rosa Ester Forgione, Barbara A. Bensing, Koichi Fukase, Antonio Molinaro, Andrea Bosso, Shinji Yokoyama, Di Carluccio, C., Forgione, R. E., Bosso, A., Yokoyama, S., Manabe, Y., Pizzo, E., Molinaro, A., Fukase, K., Fragai, M., Bensing, B. A., Marchetti, R., and Silipo, A.
Subjects: 0303 health sciences, Glycan, biology, Streptococcus gordonii, SIGLEC, 010402 general chemistry, biology.organism_classification, Oral cavity, 01 natural sciences, Biochemistry, Genetics and Molecular Biology (miscellaneous), Biochemistry, 0104 chemical sciences, 3. Good health, Microbiology, Bacterial adhesin, Chemistry, 03 medical and health sciences, Strain specificity, Streptococcus sanguinis, Molecular recognition, Chemistry (miscellaneous), biology.protein, Molecular Biology, 030304 developmental biology
Abstract: Streptococcus gordonii and Streptococcus sanguinis, commensal bacteria present in the oral cavity of healthy individuals, upon entry into the bloodstream can become pathogenic, causing infective endocarditis (IE). Sialic acid-binding serine-rich repeat adhesins on the microbial surface represent an important factor of successful infection to cause IE. They contain Siglec-like binding regions (SLBRs) that variously recognize different repertoires of O-glycans, with some strains displaying high selectivity and others broader specificity. We here dissect at an atomic level the mechanism of interaction of SLBR-B and SLBR-H from S. gordonii with a multivarious approach that combines NMR spectroscopy and computational and biophysical studies. The binding pockets of both SLBRs are broad enough to accommodate extensive interactions with sialoglycans although with key differences related to strain specificity. Furthermore, and significantly, the pattern of interactions established by the SLBRs are mechanistically very different from those reported for mammalian Siglecs despite them having a similar fold. Thus, our detailed description of the binding modes of streptococcal Siglec-like adhesins sparks the development of tailored synthetic inhibitors and therapeutics specific for Streptococcal adhesins to counteract IE, without impairing the interplay between Siglecs and glycans., We here present a detailed molecular description of sialoglycans recognition by Siglec-like adhesins from S. gordonii opening the venue for the design of specific inhibitors to influence the propensity of streptococci to cause infective endocarditis.
Published: 2021
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3. The ribotoxin-like protein Ostreatin from Pleurotus ostreatus fruiting bodies: Confirmation of a novel ribonuclease family expressed in basidiomycetes

Author: Sara Ragucci, Mariangela Valletta, Nicola Landi, Elio Pizzo, Antimo Di Maro, Rosita Russo, J. Miguel Ferreras, Landi, N., Ragucci, S., Russo, R., Valletta, M., Pizzo, E., Ferreras, J. M., and Di Maro, A.
Subjects: Models, Molecular, Protein Conformation, Gene Expression, 02 engineering and technology, Pleurotus, Biochemistry, Ribotoxin-like protein, Ribonuclease, Structure-Activity Relationship, 03 medical and health sciences, Ribonucleases, Ascomycota, Structural Biology, Catalytic triad, Protein biosynthesis, Amino Acid Sequence, Fruiting Bodies, Fungal, Homology modeling, Ageritin, Molecular Biology, Peptide sequence, 030304 developmental biology, Mycotoxin, 0303 health sciences, Base Sequence, biology, Chemistry, Agrocybe, Agaricale, Protein primary structure, General Medicine, Mycotoxins, Recombinant Protein, 021001 nanoscience & nanotechnology, biology.organism_classification, Recombinant Proteins, Ribotoxin-like proteins, Enzyme Activation, Pleurotus ostreatu, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Chromatography, Gel, biology.protein, Pleurotus ostreatus, Agaricales, Pleurotu, 0210 nano-technology
Abstract: Fungi produce several toxins active against plants, animal or humans. Among them, ribotoxins are enzymes that specifically attack ribosomes irreparably compromising protein synthesis, useful as insecticides or as anticancer agents. Here, a novel ribotoxin from the edible mushroom Pleurotus ostreatus has been purified and characterized. This ribotoxin, named Ostreatin, is a specific ribonuclease releasing α-fragment when incubated with yeast or rabbit ribosomes. Ostreatin shows IC50 of 234 pM in rabbit reticulocyte lysate, and metal dependent endonuclease activity. Following the completion of Ostreatin primary structure, we ascertained that this toxin is homologous to Ageritin, the first ribotoxin-like protein from the basidiomycete Agrocybe aegerita, with which it shares 38.8% amino acid sequence identity. Ostreatin consists of 131 amino acid residues with an experimental molecular mass of 14,263.51 Da ([M+H+]+). Homology modeling revealed that Ostreatin and Ageritin share a similar fold in which the common catalytic triad is conserved. Purified Ostreatin lacks N-terminal and C-terminal peptides, which instead are present in the Ostreatin coding sequence. Such peptides are probably involved in protein sorting and for this they could be removed. Our findings confirm the presence of ribotoxin-like proteins in basidiomycetes edible mushrooms, that we propose as novel tool for biotechnological applications.
Published: 2020
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4. Glucose‐regulated protein ( <scp>GRP78</scp> ) is an important cell surface receptor for viral invasion, cancers, and neurological disorders

Author: Udhayakumar Gopal, Salvatore V. Pizzo, Richard C. Austin, and Mario Gonzalez-Gronow
Subjects: 0301 basic medicine, Cell Survival, Glucose-regulated protein, Clinical Biochemistry, Nerve Tissue Proteins, Receptors, Cell Surface, Exosomes, GPI-Linked Proteins, Ligands, Cripto, Autoantigens, Biochemistry, 03 medical and health sciences, Autoimmune Diseases of the Nervous System, 0302 clinical medicine, Protein Domains, Cell surface receptor, Heat shock protein, Tumor Microenvironment, Genetics, Humans, Neoplasm Invasiveness, Receptor, Endoplasmic Reticulum Chaperone BiP, Molecular Biology, Heat-Shock Proteins, Autoantibodies, biology, SARS-CoV-2, Chemistry, Endoplasmic reticulum, COVID-19, Cell Biology, Virus Internalization, Endoplasmic Reticulum Stress, Neoplasm Proteins, Transport protein, Cell biology, Protein Transport, 030104 developmental biology, 030220 oncology & carcinogenesis, Spike Glycoprotein, Coronavirus, Unfolded Protein Response, biology.protein, Receptors, Virus, Signal transduction, Signal Transduction
Abstract: The 78 kDa glucose-regulated protein (GRP78) is an endoplasmic reticulum (ER)-resident molecular chaperone. GRP78 is a member of the 70 kDa heat shock family of proteins involved in correcting and clearing misfolded proteins in the ER. In response to cellular stress, GRP78 escapes from the ER and moves to the plasma membrane where it (a) functions as a receptor for many ligands, and (b) behaves as an autoantigen for autoantibodies that contribute to human disease and cancer. Cell surface GRP78 (csGRP78) associates with the major histocompatibility complex class I (MHC-I), and is the port of entry for several viruses, including the predictive binding of the novel SARS-CoV-2. Furthermore, csGRP78 is found in association with partners as diverse as the teratocarcinoma-derived growth factor 1 (Cripto), the melanocortin-4 receptor (MC4R) and the DnaJ-like protein MTJ-1. CsGRP78 also serves as a receptor for a large variety of ligands including activated α2 -macroglobulin (α2 M*), plasminogen kringle 5 (K5), microplasminogen, the voltage-dependent anion channel (VDAC), tissue factor (TF), and the prostate apoptosis response-4 protein (Par-4). In this review, we discuss the mechanisms involved in the translocation of GRP78 from the ER to the cell surface, and the role of secreted GRP78 and its autoantibodies in cancer and neurological disorders.
Published: 2021
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5. Mycobacterium tuberculosis Immune Response in Patients With Immune-Mediated Inflammatory Disease

Author: Elisa Petruccioli, Linda Petrone, Teresa Chiacchio, Chiara Farroni, Gilda Cuzzi, Assunta Navarra, Valentina Vanini, Umberto Massafra, Marianna Lo Pizzo, Giuliana Guggino, Nadia Caccamo, Fabrizio Cantini, Fabrizio Palmieri, Delia Goletti, Petruccioli E., Petrone L., Chiacchio T., Farroni C., Cuzzi G., Navarra A., Vanini V., Massafra U., Lo Pizzo M., Guggino G., Caccamo N., Cantini F., Palmieri F., and Goletti D.
Subjects: Tuberculosis, Immunology, Population, chemical and pharmacologic phenomena, Disease, Mycobacterium tuberculosis, Immune system, medicine, M. tuberculosis, Immunology and Allergy, Cytotoxic T cell, education, IFN-γ, CD27, Original Research, education.field_of_study, biology, business.industry, RC581-607, bacterial infections and mycoses, medicine.disease, biology.organism_classification, tuberculosis, Rheumatoid arthritis, Tumor necrosis factor alpha, Immunologic diseases. Allergy, business, immune-mediated inflammatory disease
Abstract: Subjects with immune-mediated inflammatory diseases (IMID), such as rheumatoid arthritis (RA), have an intrinsic higher probability to develop active-tuberculosis (TB) compared to the general population. The risk ranges from 2.0 to 8.9 in RA patients not receiving therapies. According to the WHO, the RA prevalence varies between 0.3% and 1% and is more common in women and in developed countries. Therefore, the identification and treatment of TB infection (TBI) in this fragile population is important to propose the TB preventive therapy. We aimed to study the M. tuberculosis (Mtb) specific T-cell response to find immune biomarkers of Mtb burden or Mtb clearance in patients with different TB status and different risk to develop active-TB disease. We enrolled TBI subjects as example of Mtb-containment, the active-TB as example of a replicating Mtb status, and the TBI-IMID as fragile population. To study the Mtb-specific response in a condition of possible Mtb sterilization, we longitudinally enrolled TBI subjects and active-TB patients before and after TB therapy. Peripheral blood mononuclear cells were stimulated overnight with Mtb peptides contained in TB1- and TB2-tubes of the Quantiferon-Plus kit. Then, we characterized by cytometry the Mtb-specific CD4 and CD8 T cells. In TBI-IMID, the TB therapy did not affect the ability of CD4 T cells to produce interferon-γ, tumor necrosis factor-α, and interleukin-2, their functional status, and their phenotype. The TB therapy determined a contraction of the triple functional CD4 T cells of the TBI subjects and active-TB patients. The CD45RA- CD27+ T cells stood out as a main subset of the Mtb-specific response in all groups. Before the TB-preventive therapy, the TBI subjects had higher proportion of Mtb-specific CD45RA-CD27+CD4+ T cells and the active-TB subjects had higher proportion of Mtb-specific CD45RA-CD27-CD4+ T cells compared to other groups. The TBI-IMID patients showed a phenotype similar to TBI, suggesting that the type of IMID and the IMID therapy did not affect the activation status of Mtb-specific CD4 T cells. Future studies on a larger and better-stratified TBI-IMID population will help to understand the change of the Mtb-specific immune response over time and to identify possible immune biomarkers of Mtb-containment or active replication.
Published: 2021

6. Antibodies Responses to SARS-CoV-2 in a Large Cohort of Vaccinated Subjects and Seropositive Patients

Author: Francesco Vitale, Stefano Pizzo, Giuseppe Calamusa, Dario Genovese, Alessandra Casuccio, Donatella Ferraro, Emanuele Amodio, Floriana Bonura, Giuseppina Capra, Giovanni M. Giammanco, Simona De Grazia, Amodio, Emanuele, Capra, Giuseppina, Casuccio, Alessandra, Grazia, Simona De, Genovese, Dario, Pizzo, Stefano, Calamusa, Giuseppe, Ferraro, Donatella, Giammanco, Giovanni Maurizio, Vitale, Francesco, and Bonura, Floriana
Subjects: 0301 basic medicine, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), viruses, Immunology, Article, Serology, Persistence (computer science), 03 medical and health sciences, 0302 clinical medicine, Antigen, Drug Discovery, Medicine, Pharmacology (medical), 030212 general & internal medicine, skin and connective tissue diseases, Pharmacology, antibody concentrations, biology, business.industry, Immunogenicity, SARS-CoV-2 infection, fungi, respiratory tract diseases, Vaccination, body regions, 030104 developmental biology, Infectious Diseases, Immunization, biology.protein, Antibody, business, COVID-19 vaccine
Abstract: COVID-19 is a current global threat, and the characterization of antibody response is vitally important to update vaccine development and strategies. In this study we assessed SARS-CoV-2 antibody concentrations in SARS-CoV-2 positive patients (N = 272) and subjects vaccinated with the BNT162b2 m-RNA COVID-19 vaccine (N = 1256). For each participant, socio-demographic data, COVID-19 vaccination records, serological analyses, and SARS-CoV-2 infection status were collected. IgG antibodies against S1/S2 antigens of SARS-CoV-2 were detected. Almost all vaccinated subjects (99.8%) showed a seropositivity to anti-SARS-COV-2 IgG and more than 80% of vaccinated subjects had IgG concentrations &gt, 200 AU/mL. In a Tobit multivariable regression analysis, SARS-CoV-2 vaccination was statistically significantly associated with increased IgG concentrations (β coef = 266.4, p &lt, 0.001). A statistically significant reduction in SARS-CoV-2 IgG concentrations was found with older age (β coef = −1.96 per year increase, 0.001), male sex (β coef = −22.3, 0.001), and days after immunization (β coef = −1.67 per day increase, 0.001). Our findings could support the vaccination campaigns confirming the high immunogenicity of the SARS-CoV-2 vaccine under investigation with respect to the natural infection. Further studies will be required for evaluating the role of age and days after immunization in the persistence of vaccine antibodies and protection from the disease.
Published: 2021

7. Enzymes as a Reservoir of Host Defence Peptides

Author: Alberto Di Donato, Elio Pizzo, Antimo Di Maro, Valeria Cafaro, Andrea Bosso, Eugenio Notomista, Bosso, Andrea, Di Maro, Antimo, Cafaro, Valeria, Di Donato, Alberto, Notomista, Eugenio, Pizzo, Elio, Bosso, A., Di Maro, A., Cafaro, V., Di Donato, A., Notomista, E., and Pizzo, E.
Subjects: Hydrolases, Protein Conformation, Proteolysis, Hydrolase, proteolysi, Computational biology, Biology, immunomodulation, 03 medical and health sciences, Enzyme activator, Protein structure, medicine, Humans, Structure–activity relationship, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Antimicrobial Cationic Peptide, Innate immune system, medicine.diagnostic_test, 030306 microbiology, Drug discovery, Hydrolysis, structure-activity relationship, mimetic peptide, Biocatalysi, General Medicine, Host defence, Hydrolysi, Immunity, Innate, Enzyme Activation, Enzyme, chemistry, Oxidoreductase, Biocatalysis, Oxidoreductases, Antimicrobial Cationic Peptides, Human
Abstract: Host defence peptides (HDPs) are powerful modulators of cellular responses to various types of insults caused by pathogen agents. To date, a wide range of HDPs, from species of different kingdoms including bacteria, plant and animal with extreme diversity in structure and biological activity, have been described. Apart from a limited number of peptides ribosomally synthesized, a large number of promising and multifunctional HDPs have been identified within protein precursors, with properties not necessarily related to innate immunity, consolidating the fascinating hypothesis that proteins have a second or even multiple biological mission in the form of one or more bio-active peptides. Among these precursors, enzymes constitute certainly an interesting group, because most of them are mainly globular and characterized by a fine specific internal structure closely related to their catalytic properties and also because they are yet little considered as potential HDP releasing proteins. In this regard, the main aim of the present review is to describe a panel of HDPs, identified in all canonical classes of enzymes, and to provide a detailed description on hydrolases and their corresponding HDPs, as there seems to exist a striking link between these structurally sophisticated catalysts and their high content in cationic and amphipathic cryptic peptides.
Published: 2020

8. Effect of an additional N-terminal methionyl residue on enzymatic and antifungal activities of Ageritin purified from Agrocybe aegerita fruiting bodies

Author: Lucía Citores, Rosita Russo, Elio Pizzo, Antimo Di Maro, Rosario Iglesias, Mariangela Valletta, Paolo V. Pedone, Sara Ragucci, Nicola Landi, Ragucci, S, Landi, N, Russo, R, Valletta, M, Citores, L, Iglesias, R, Pedone, Pv, Pizzo, E, Di Maro, A, Ragucci, S., Landi, N., Russo, R., Valletta, M., Citores, L., Iglesias, R., Pedone, P. V., Pizzo, E., and Di Maro, A.
Subjects: Antifungal Agents, Protein Conformation, Saccharomyces cerevisiae, 02 engineering and technology, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Endonuclease, Ribonucleases, Structural Biology, Protein biosynthesis, Agrocybe, Antifungal activity, Ribonuclease, Fruiting Bodies, Fungal, Molecular Biology, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, Agrocybe aegerita, General Medicine, 021001 nanoscience & nanotechnology, biology.organism_classification, Yeast, Enzyme, Ricin, chemistry, biology.protein, Additional N-terminal methionyl residue, 0210 nano-technology
Abstract: Ageritin, a specific ribonuclease, damaging the largest rRNA in the highly conserved α-sarcin/ricin stem-loop (SRL) has been well characterized from edible mushroom Agrocybe aegerita. Given its peculiar characteristic, Ageritin is the prototype of a new ribotoxins family expressed in basidiomycetes. In this framework, we report the characterization of Met-Ageritin, an isoform of Ageritin with an additional N-terminal methionyl residue. This difference affects the enzymatic features of this toxin despite is able to release α-fragment when acting on yeast, rabbit or Trichoderma asperellum ribosomes. Met-Ageritin inhibits protein synthesis in vitro with an IC50 = 2.8 nM that is 21-fold lower than that of Ageritin, while not show endonuclease activity on DNA. Subsequently, we explored the antifungal activity of both isoforms against T. asperellum, pathogen for A. aegerita and Saccharomyces cerevisiae, used as eukaryotic model microorganism. The presence of an additional N-terminal methionyl residue in Met-Ageritin abolishes antifungal activity towards T. asperellum, while neither of two isoforms is able to inhibit the growth of S. cerevisiae. Overall, these data highlight the importance of the N-terminal region of this toxin that likely alters the conformational state of this enzyme considering the presence in this region of metal binding sites necessary for explicate enzymatic activity.
Published: 2020

9. Cost-effective production of recombinant peptides in Escherichia coli

Author: Angela Arciello, Eugenio Notomista, Eliana Dell’Olmo, Rosa Gaglione, Elio Pizzo, Valeria Cafaro, Katia Pane, Giuseppe Olivieri, Gaglione, Rosa, Pane, Katia, Dell'Olmo, Eliana, Cafaro, Valeria, Pizzo, Elio, Olivieri, Giuseppe, Notomista, Eugenio, and Arciello, Angela
Subjects: 0106 biological sciences, Bio Process Engineering, Cost-Benefit Analysis, Bioengineering, Industrial fermentation, medicine.disease_cause, 01 natural sciences, law.invention, 03 medical and health sciences, Bioreactors, law, 010608 biotechnology, Escherichia coli, Cationic Antimicrobial Peptides, medicine, Production (economics), Techno-economic analysi, Cost-effective recombinant production, Molecular Biology, Techno-economic analysis, 030304 developmental biology, 0303 health sciences, Auto-inducing expression procedure, Apolipoprotein A-I, biology, Recombinant expression, Host defence peptides, General Medicine, Host defence, biology.organism_classification, Recombinant Proteins, Host defence peptide, Biochemistry, Recombinant DNA, Peptides, Apolipoprotein B, Bacteria, Biotechnology
Abstract: Among bioactive peptides, cationic antimicrobial peptides (AMPs), also referred to as host defence peptides (HDPs), are valuable tools to treat infections, being able to kill a wide variety of microbes directly and/or modulate host immunity. HDPs have great therapeutic potential against antibiotic-resistant bacteria, viruses and even parasites. However, high manufacturing costs have greatly limited their development as drugs, thus highlighting the need to develop novel and competitive production strategies. Here, a cost-effective procedure was established to produce the high amounts of peptides required for basic and clinical research. Firstly, a novel culture medium was designed, which was found to support significantly higher cell densities and recombinant expression levels of peptides under test compared to conventional media. The procedure has been also efficiently scaled up by using a 5 L fermenter, while the costs have been lowered significantly by developing a successful auto-induction strategy, which has been found to support higher yields of target constructs and cell biomass compared to conventional strategies based on expression induction by IPTG. Interestingly, it was estimated that by increasing production scale from 100 to 1000 mg/batch, unit costs decreased strongly from 253 to 42 €/mg. These costs appear highly competitive when compared to chemical synthesis strategies. Altogether, the data indicate that the strategy represents an important starting point for the future development of large-scale manufacture of HDPs. © 2019 Elsevier B.V.
Published: 2019
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10. Molecular and cellular analysis of orange plants infected with Huanglongbing (citrus greening disease)

Author: Tricia L. Meredith, Nicholas Pizzo, Mohamed Abutineh, Xing-Hai Zhang, John M. Harlin, Xiao-Lu Jin, Sarah Naylon, and Lyndon M. West
Subjects: 0106 biological sciences, 0301 basic medicine, biology, Physiology, fungi, food and beverages, Plant physiology, Plant Science, Orange (colour), biology.organism_classification, 01 natural sciences, Plant disease, Microbiology, 03 medical and health sciences, 030104 developmental biology, Citrus greening disease, Phloem, Agronomy and Crop Science, Gene, Prophage, Bacteria, 010606 plant biology & botany
Abstract: Huanglongbing (HLB, also commonly known as citrus greening disease) is caused by the bacterium Candidatus Liberibacter asiaticus (CLas) in the US. It is a serious plant disease causing tremendous economic damages and posing an existential threat to the citrus industry worldwide. CLas proliferates inside the phloem, clogs the transportation system, stunts plant growth and renders trees barren. Currently there is no cure or effective treatments for this disease. In this study, qPCR and scanning electron microscopy (SEM) were used to examine orange plants with or without HLB symptoms. We found that symptomatic HLB plants showed high levels of CLas DNA and its prophage in leaves and had heavily clogged phloem tissues. In contrast, the asymptomatic, healthy looking plants had detectable, low levels of CLas and prophage DNA by qPCR but the SEM imaging revealed phloem clear of clogging deposits. Transcription of several CLas phage genes was detected in both healthy and diseased plants, however, higher transcription levels were observed in the healthy plants than in the diseased plants. As part of our efforts to explore the possibility of using a plant-based antibacterial concoction named Agent G to mitigate HLB, NMR and GC/MS were used to assess its organic chemical composition and migration through the phloem tissue. It was found that the major compounds of Agent G were allyl polysulfides and cinnamaldehyde. The phloemic migrate rate in planta was estimated between 1.5 and 3.25 cm/h. Our studies suggest that a combination of qPCR test and SEM imaging may prove to be more informative for gauging growth status of citrus plants and for early HLB detection. We also showcase a feasible approach of treating HLB by delivering antibacterial reagents directly into the phloem tissue where most CLas reside.
Published: 2020
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11. Lipid profile and fatty acid composition of marine fish species from Northeast coast of Brazil

Author: Isabella Peres Gualda, Renata Menoci Gonçalves, Paula Fernandes Montanher, Jesuí Vergílio Visentainer, Maria Eugênia Petenuci, Marília Bellanda Galuch, Fabiana Carla Maistrovicz, and Jessica S. Pizzo
Subjects: chemistry.chemical_classification, 0303 health sciences, medicine.diagnostic_test, 030309 nutrition & dietetics, Daily intake, 010401 analytical chemistry, Marine fish, Nutritional quality, Biology, 01 natural sciences, 0104 chemical sciences, 03 medical and health sciences, chemistry, Lipid content, medicine, Original Article, lipids (amino acids, peptides, and proteins), Fatty acid composition, Food science, Gas chromatography, Lipid profile, Food Science, Polyunsaturated fatty acid
Abstract: Total lipid content, fatty acid composition and nutritional profile of lipid fraction of fourteen fish species from the Brazilian Northeastern coast were evaluated. Lipid content was determined by Bligh and Dyer methodology, whereas the fatty acid composition was determined by gas chromatography with flame ionization detector. The indices of atherogenicity, thrombogenicity and hypocholesterolemic/hypercholesterolemic ratio were used to evaluate the nutritional quality of lipid fraction. The total lipid content ranged from 0.25 to 3.09%, with higher values in L. synagris. A significant difference (p
Published: 2020
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12. Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease

Author: Hermann C. Altmeppen, Christina J. Sigurdson, Timothy D. Kurt, Donald P. Pizzo, Sofie Nyström, Thu H Nam, Katrin Soldau, Jeffrey D. Esko, K. Peter R. Nilsson, Taylor Schumann, Jessica Lawrence, Markus Glatzel, Patricia Aguilar-Calvo, Biswa Choudhury, and Alejandro M. Sevillano
Subjects: 0301 basic medicine, animal diseases, Glycobiology, Oligosaccharides, Neurodegenerative, Medical and Health Sciences, Transgenic, Prion Diseases, Mice, chemistry.chemical_compound, 0302 clinical medicine, 2.1 Biological and endogenous factors, Aetiology, Dominance (genetics), Infectious disease, biology, Neurodegeneration, Brain, General Medicine, Heparan sulfate, Phenotype, Cell biology, Infectious Diseases, 030220 oncology & carcinogenesis, Neurological, Research Article, Glycan, Prions, Immunology, Mutation, Missense, Mice, Transgenic, Protein Aggregation, Pathological, Prion Proteins, 03 medical and health sciences, Rare Diseases, Pathological, Polysaccharides, medicine, Extracellular, Animals, Protein Processing, Post-Translational, Transmissible Spongiform Encephalopathy (TSE), medicine.disease, Protein Aggregation, Brain Disorders, nervous system diseases, Emerging Infectious Diseases, 030104 developmental biology, Amino Acid Substitution, chemistry, Mutation, Commentary, biology.protein, Missense, Protein Processing, Post-Translational, Neuroscience, Spongiosis
Abstract: Posttranslational modifications (PTMs) are common among proteins that aggregate in neurodegenerative disease, yet how PTMs impact the aggregate conformation and disease progression remains unclear. By engineering knockin mice expressing prion protein (PrP) lacking 2 N-linked glycans (Prnp(180Q/196Q)), we provide evidence that glycans reduce spongiform degeneration and hinder plaque formation in prion disease. Prnp(180Q/196Q) mice challenged with 2 subfibrillar, non–plaque-forming prion strains instead developed plaques highly enriched in ADAM10-cleaved PrP and heparan sulfate (HS). Intriguingly, a third strain composed of intact, glycophosphatidylinositol-anchored (GPI-anchored) PrP was relatively unchanged, forming diffuse, HS-deficient deposits in both the Prnp(180Q/196Q) and WT mice, underscoring the pivotal role of the GPI-anchor in driving the aggregate conformation and disease phenotype. Finally, knockin mice expressing triglycosylated PrP (Prnp(187N)) challenged with a plaque-forming prion strain showed a phenotype reversal, with a striking disease acceleration and switch from plaques to predominantly diffuse, subfibrillar deposits. Our findings suggest that the dominance of subfibrillar aggregates in prion disease is due to the replication of GPI-anchored prions, with fibrillar plaques forming from poorly glycosylated, GPI-anchorless prions that interact with extracellular HS. These studies provide insight into how PTMs impact PrP interactions with polyanionic cofactors, and highlight PTMs as a major force driving the prion disease phenotype.
Published: 2020
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13. Tumor necrosis factor receptor-1 is selectively sequestered into Schwann cell extracellular vesicles where it functions as a TNFα decoy

Author: Stefano Martellucci, Seiji Ohtori, Naoya Hirosawa, Steven L. Gonias, Jasmine Le, Donald P. Pizzo, Mahrou Sadri, Hyo Jun Kwon, Haylie Romero, and Wendy M. Campana
Subjects: Tumor Necrosis Factor-alpha, p38 mitogen-activated protein kinases, Schwann cell, Biological activity, respiratory system, Biology, In vitro, Cell biology, Cellular and Molecular Neuroscience, Extracellular Vesicles, medicine.anatomical_structure, Neurology, In vivo, Receptors, Tumor Necrosis Factor, Type I, medicine, Phosphorylation, Receptors, Tumor Necrosis Factor, Type II, Tumor necrosis factor alpha, Tumor necrosis factor receptor 1, Schwann Cells, extracellular vesicles, neuropathic pain, peripheral nerve injury, schwann cells, tnf receptor-1, tnfα, Cells, Cultured
Abstract: Schwann cells (SCs) are known to produce extracellular vesicles (EV) that participate in cell-cell communication by transferring cargo to target cells, including mRNAs, microRNAs, and biologically active proteins. Herein, we report a novel mechanism whereby SC EVs may regulate PNS physiology, especially in injury, by controlling the activity of TNFα. SCs actively sequester tumor necrosis factor receptor-1 (TNFR1) into EVs at high density, accounting for about 2% of the total protein in SC EVs (~1000 copies TNFR1/EV). Although TNFR2 was robustly expressed by SCs in culture, TNFR2 was excluded from SC EVs. SC EV TNFR1 bound TNFα, decreasing the concentration of free TNFα available to bind to cells and thus served as a TNFα decoy. SC EV TNFR1 significantly inhibited TNFα-induced p38 MAPK phosphorylation in cultured SCs. When TNFR1 was proteolytically removed from SC EVs using tumor necrosis factor-α converting enzyme (TACE) or neutralized with antibody, the ability of TNFα to activate p38 MAPK in the presence of these EVs was restored. As further evidence of its decoy activity, SC EV TNFR1 modified TNFα activities in vitro including: (1) regulation of expression of other cytokines; (2) effects on SC morphology; and (3) effects on SC viability. SC EVs also modified the effects of TNFα on sciatic nerve morphology and neuropathic pain-related behavior in vivo. By sequestering TNFR1 in EVs, SCs may buffer against the potentially toxic effects of TNFα. SC EVs provide a novel mechanism for the spatial and temporal regulation of neuro-inflammation.
Published: 2022

14. A case of infective colitis due to Yersinia enterocolitica complicated by microliver abscesses mimicking multiple liver occult metastases: a case report

Author: Marco Cataldi, Giuseppe Brancatelli, Chiara Pintus, Antonino Tuttolomondo, Valerio Vassallo, Salvatore Miceli, Rosario Luca Norrito, Mario Daidone, Maria Grazia Puleo, Alessandro Del Cuore, Tiziana Di Chiara, G. Pizzo, Antonio Pinto, Norrito R.L., Pintus C., Cataldi M., Del Cuore A., Daidone M., Vassallo V., Puleo M.G., Di Chiara T., Miceli S., Pizzo G.M., Brancatelli G., Tuttolomondo A., and Pinto A.
Subjects: 0301 basic medicine, medicine.medical_specialty, Settore MED/09 - Medicina Interna, Case report, Infective colitis, Microliver abscesses, Yersinia enterocolitica, Aged, Anti-Bacterial Agents, Bacteremia, Liver Neoplasms, Treatment Outcome, Yersinia Infections, Colitis, Diagnosis, Differential, Female, Humans, Liver Abscess, Yersinia Infections, 030106 microbiology, Liver Abscess, Infective colitis, Case Report, Bacteremia, Infectious and parasitic diseases, RC109-216, Inflammatory bowel disease, Gastroenterology, Metastasis, Diagnosis, Differential, 03 medical and health sciences, 0302 clinical medicine, Medical microbiology, Internal medicine, medicine, Humans, 030212 general & internal medicine, Yersinia enterocolitica, Aged, Doxycycline, biology, business.industry, Liver Neoplasms, Microliver abscesses, medicine.disease, biology.organism_classification, Colitis, Occult, Anti-Bacterial Agents, Infectious Diseases, Treatment Outcome, Female, Differential diagnosis, business, Cefixime, medicine.drug
Abstract: Background We report an unusual case of infective colitis by Yersinia enterocolitica complicated by microliver abscesses mimicking multiple liver metastases in a 79 yr old female without any risk factors for bacteriaemia by this pathogen. Case presentation The patient was admitted to the Internal Medicine with Stroke Care ward of University Policlinico “P. Giaccone” in Palermo because of the appearance of diarrhoea. After the antimicrobial treatment for infective colitis, the clinicians observed a persistently increased white blood cells (WBC) count and multiple hepatic lesions; after having excluded any neoplastic disease and inflammatory bowel disease (IBD), blood cultures positive for Y. enterocolitica allowed to establish the final diagnosis was infective micro liver abscesses consequent to infective colitis due to Y. enterocolitica, which were successfully treated with cefixime and doxycycline. Conclusions This case report should make clinicians reflect on how complex the differential diagnosis between microliver abscesses and metastasis could be and the possibility of bacteriaemia by Y. enterocolitica even without iron overload conditions.
Published: 2021

15. Safety and efficacy of a feed additive consisting of Saccharomyces cerevisiae MUCL 39885 (Biosprint®) for cats and dogs (Prosol S.p.A.)

Author: Montserrat Anguita, Yolanda Sanz, Maria de Lourdes Bastos, Maryline Kouba, Marta López-Alonso, Alena Pechová, Ruud Woutersen, Birgit Dusemund, Elisa Pettenati, Jordi Tarrés-Call, Fabiola Pizzo, Baltasar Mayo, Giovanna Martelli, Jaume Galobart, Mariana Petkova, Fernando Ramos, Efsa Panel on Additives, Roberto Edoardo Villa, Paola Manini, Giovanna Azimonti, Francesca Marcon, Henrik Christensen, Vasileios Bampidis, Secundino López Puente, Mojca Fašmon Durjava, Bampidis V., Azimonti G., Bastos M.D.L., Christensen H., Dusemund B., Fasmon Durjava M., Kouba M., Lopez-Alonso M., Lopez Puente S., Marcon F., Mayo B., Pechova A., Petkova M., Ramos F., Sanz Y., Villa R.E., Woutersen R., Martelli G., Anguita M., Galobart J., Manini P., Tarres-Call J., Pettenati E., and Pizzo F.
Subjects: dogs, Veterinary (miscellaneous), Feed additive, Saccharomyces cerevisiae, cat, Plant Science, TP1-1185, ®, Safety status, Microbiology, QPS, Anim2953, Animal science, Biosprint®, TX341-641, renewal, CATS, biology, Nutrition. Foods and food supply, Chemical technology, cats, biology.organism_classification, Scientific Opinion, zootechnical additive, dog, Animal Science and Zoology, Parasitology, Biosprint, Food Science
Abstract: The additive Biosprint® contains viable cells of Saccharomyces cerevisiae MUCL 39885 and is authorised as a feed additive in sows, dairy cows, horses, piglets (weaned), cattle for fattening, minor ruminants for fattening and minor ruminants for dairy products. The applicant has requested to extend the use of the additive to cats and dogs at a minimum inclusion level of 7 × 1010 CFU/kg of complete feed. S. cerevisiae is considered by EFSA to have qualified presumption of safety status and consequently is considered safe for the target species. The additive is considered as a potential skin and eye irritant and a skin and respiratory sensitiser. Based on the results on efficacy studies provided, the FEEDAP Panel concludes that Biosprint® is efficacious when used in feeds for dogs. However, the FEEDAP Panel considered that the biological relevance of the magnitude of the effect detected is questionable. Based on the trial available, the FEEDAP Panel was unable to conclude on the efficacy of the additive when administered to cats.
Published: 2021
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16. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author: Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, 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Karolina, Piya, Sujan, Pizzo, Paola, Plantinga, Theo, Platta, Harald, Plaza-Zabala, Ainhoa, Plomann, Markus, Plotnikov, Egor, Plun-Favreau, Helene, Pluta, Ryszard, Pocock, Roger, Pöggeler, Stefanie, Pohl, Christian, Poirot, Marc, Poletti, Angelo, Ponpuak, Marisa, Popelka, Hana, Popova, Blagovesta, Porta, Helena, Porte Alcon, Soledad, Portilla-Fernandez, Eliana, Post, Martin, Potts, Malia, Poulton, Joanna, Powers, Ted, Prahlad, Veena, Prajsnar, Tomasz, Praticò, Domenico, Prencipe, Rosaria, Priault, Muriel, Proikas-Cezanne, Tassula, Promponas, Vasilis, Proud, Christopher, Puertollano, Rosa, Puglielli, Luigi, Pulinilkunnil, Thomas, Puri, Deepika, Puri, Rajat, Puyal, Julien, Qi, Xiaopeng, Qi, Yongmei, Qian, Wenbin, Qiang, Lei, Qiu, Yu, Quadrilatero, Joe, Quarleri, Jorge, Raben, Nina, Rabinowich, Hannah, Ragona, Debora, Ragusa, Michael, Rahimi, Nader, Rahmati, Marveh, Raia, Valeria, Raimundo, Nuno, Rajasekaran, Namakkal-Soorappan, Ramachandra Rao, Sriganesh, Rami, Abdelhaq, Ramírez-Pardo, Ignacio, Ramsden, David, Randow, Felix, Rangarajan, Pundi, Ranieri, Danilo, Rao, Hai, Rao, Lang, Rao, Rekha, Rathore, Sumit, Ratnayaka, J Arjuna, Ratovitski, Edward, Ravanan, Palaniyandi, Ravegnini, Gloria, Ray, Swapan, Razani, Babak, Rebecca, Vito, Reggiori, Fulvio, Régnier-Vigouroux, Anne, Reichert, Andreas, Reigada, David, Reiling, Jan, Rein, Theo, Reipert, Siegfried, Rekha, Rokeya Sultana, Ren, Hongmei, Ren, Jun, Ren, Weichao, Renault, Tristan, Renga, Giorgia, Reue, Karen, Rewitz, Kim, Ribeiro de Andrade Ramos, Bruna, Riazuddin, S Amer, Ribeiro-Rodrigues, Teresa, Ricci, Jean-Ehrland, Ricci, Romeo, Riccio, Victoria, Richardson, Des, Rikihisa, Yasuko, Risbud, Makarand, Risueño, Ruth, Ritis, Konstantinos, Rizza, Salvatore, Rizzuto, Rosario, Roberts, Helen, Roberts, Luke, Robinson, Katherine, Roccheri, Maria Carmela, Rocchi, Stephane, Rodney, George, Rodrigues, Tiago, Rodrigues Silva, Vagner Ramon, Rodriguez, Amaia, Rodriguez-Barrueco, Ruth, Rodriguez-Henche, Nieves, Rodriguez-Rocha, Humberto, Roelofs, Jeroen, Rogers, Robert, Rogov, Vladimir, ROJO, Ana, Rolka, Krzysztof, Romanello, Vanina, Romani, Luigina, Romano, Alessandra, Romano, Patricia, Romeo-Guitart, David, Romero, Luis, Romero, Montserrat, Roney, Joseph, Rongo, Christopher, Roperto, Sante, Rosenfeldt, Mathias, Rosenstiel, Philip, Rosenwald, Anne, Roth, Kevin, Roth, Lynn, Roth, Steven, Rouschop, Kasper, Roussel, Benoit, Roux, Sophie, Rovere-Querini, Patrizia, Roy, Ajit, Rozieres, Aurore, Ruano, Diego, Rubinsztein, David, Rubtsova, Maria, Ruckdeschel, Klaus, Ruckenstuhl, Christoph, Rudolf, Emil, Rudolf, Rüdiger, Ruggieri, Alessandra, Ruparelia, Avnika Ashok, Rusmini, Paola, Russell, Ryan, Russo, Gian Luigi, Russo, Maria, Russo, Rossella, Ryabaya, Oxana, Ryan, Kevin, Ryu, Kwon-Yul, Sabater-Arcis, Maria, Sachdev, Ulka, Sacher, Michael, Sachse, Carsten, Sadhu, Abhishek, Sadoshima, Junichi, Safren, Nathaniel, Saftig, Paul, Sagona, Antonia, Sahay, Gaurav, Sahebkar, Amirhossein, Sahin, Mustafa, Sahin, Ozgur, Sahni, Sumit, Saito, Nayuta, Saito, Shigeru, Saito, Tsunenori, Sakai, Ryohei, Sakai, Yasuyoshi, Sakamaki, Jun-Ichi, Saksela, Kalle, Salazar, Gloria, Salazar-Degracia, Anna, Salekdeh, Ghasem, Saluja, Ashok, Sampaio-Marques, Belém, Sanchez, Maria Cecilia, Sanchez-Alcazar, Jose, Sanchez-Vera, Victoria, Sancho-Shimizu, Vanessa, Sanderson, J Thomas, Sandri, Marco, Santaguida, Stefano, Santambrogio, Laura, Santana, Magda, Santoni, Giorgio, Sanz, Alberto, Sanz, Pascual, Saran, Shweta, Sardiello, Marco, Sargeant, Timothy, Sarin, Apurva, Sarkar, Chinmoy, Sarkar, Sovan, Sarrias, Maria-Rosa, Sarkar, Surajit, Sarmah, Dipanka Tanu, Sarparanta, Jaakko, Sathyanarayan, Aishwarya, Sathyanarayanan, Ranganayaki, Scaglione, K Matthew, Scatozza, Francesca, Schaefer, Liliana, Schafer, Zachary, Schaible, Ulrich, Schapira, Anthony, Scharl, Michael, Schatzl, Hermann, Schein, Catherine, Scheper, Wiep, Scheuring, David, Schiaffino, Maria Vittoria, Schiappacassi, Monica, Schindl, Rainer, Schlattner, Uwe, Schmidt, Oliver, Schmitt, Roland, Schmidt, Stephen, Schmitz, Ingo, Schmukler, Eran, Schneider, Anja, Schneider, Bianca, Schober, Romana, Schoijet, Alejandra, Schott, Micah, Schramm, Michael, Schröder, Bernd, Schuh, Kai, Schüller, Christoph, Schulze, Ryan, Schürmanns, Lea, Schwamborn, Jens, Schwarten, Melanie, Scialo, Filippo, Sciarretta, Sebastiano, Scott, Melanie, Scotto, Kathleen, Scovassi, A Ivana, Scrima, Andrea, Scrivo, Aurora, Sebastian, David, Sebti, Salwa, Sedej, Simon, Segatori, Laura, Segev, Nava, Seglen, Per, Seiliez, Iban, Seki, Ekihiro, Selleck, Scott, Sellke, Frank, Selsby, Joshua, Sendtner, Michael, Senturk, Serif, Seranova, Elena, Sergi, Consolato, Serra-Moreno, Ruth, Sesaki, Hiromi, Settembre, Carmine, Setty, Subba Rao Gangi, Sgarbi, Gianluca, Sha, Ou, Shacka, John, Shah, Javeed, Shang, Dantong, Shao, Changshun, Shao, Feng, Sharbati, Soroush, Sharkey, Lisa, Sharma, Dipali, Sharma, Gaurav, Sharma, Kulbhushan, Sharma, Pawan, Sharma, Surendra, Shen, Han-Ming, Shen, Hongtao, Shen, Jiangang, Shen, Ming, Shen, Weili, Shen, Zheni, Sheng, Rui, Sheng, Zhi, Sheng, Zu-Hang, Shi, Jianjian, Shi, Xiaobing, Shi, Ying-Hong, Shiba-Fukushima, Kahori, Shieh, Jeng-Jer, Shimada, Yohta, Shimizu, Shigeomi, Shimozawa, Makoto, Shintani, Takahiro, Shoemaker, Christopher, Shojaei, Shahla, Shoji, Ikuo, Shravage, Bhupendra, Shridhar, Viji, Shu, Chih-Wen, Shu, Hong-Bing, Shui, Ke, Shukla, Arvind, Shutt, Timothy, Sica, Valentina, Siddiqui, Aleem, Sierra, Amanda, Sierra-Torre, Virginia, Signorelli, Santiago, Sil, Payel, Silva, Bruno, Silva, Johnatas, Silva-Pavez, Eduardo, Silvente-Poirot, Sandrine, Simmonds, Rachel, Simon, Anna Katharina, Simon, Hans-Uwe, Simons, Matias, Singh, Anurag, Singh, Lalit, Singh, Rajat, Singh, Shivendra, Singh, Shrawan, Singh, Sudha, Singh, Sunaina, Singh, Surinder Pal, Sinha, Debasish, Sinha, Rohit Anthony, Sinha, Sangita, Sirko, Agnieszka, Sirohi, Kapil, Sivridis, Efthimios, Skendros, Panagiotis, Skirycz, Aleksandra, Slaninová, Iva, Smaili, Soraya, Smertenko, Andrei, Smith, Matthew, Soenen, Stefaan, Sohn, Eun Jung, Sok, Sophia, Solaini, Giancarlo, Soldati, Thierry, Soleimanpour, Scott, Soler, Rosa, Solovchenko, Alexei, Somarelli, Jason, Sonawane, Avinash, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Kunhua, Song, Zhiyin, Soria, Leandro, Sorice, Maurizio, Soukas, Alexander, Soukup, Sandra-Fausia, Sousa, Diana, Sousa, Nadia, Spagnuolo, Paul, Spector, Stephen, Srinivas Bharath, M., St Clair, Daret, Stagni, Venturina, Staiano, Leopoldo, Stalnecker, Clint, Stankov, Metodi, Stathopulos, Peter, Stefan, Katja, Stefan, Sven Marcel, Stefanis, Leonidas, Steffan, Joan, Steinkasserer, Alexander, Stenmark, Harald, Sterneckert, Jared, Stevens, Craig, Stoka, Veronika, Storch, Stephan, Stork, Björn, Strappazzon, Flavie, Strohecker, Anne Marie, Stupack, Dwayne, Su, Huanxing, Su, Ling-Yan, Su, Longxiang, Suarez-Fontes, Ana, Subauste, Carlos, Subbian, Selvakumar, Subirada, Paula, Sudhandiran, Ganapasam, Sue, Carolyn, Sui, Xinbing, Summers, Corey, Sun, Guangchao, Sun, Jun, SUN, Kang, Sun, Meng-xiang, Sun, Qiming, Sun, Yi, Sun, Zhongjie, Sunahara, Karen, Sundberg, Eva, Susztak, Katalin, Sutovsky, Peter, Suzuki, Hidekazu, Sweeney, Gary, Symons, J David, Sze, Stephen Cho Wing, Szewczyk, Nathaniel, Tabęcka-Łonczynska, Anna, Tabolacci, Claudio, Tacke, Frank, Taegtmeyer, Heinrich, Tafani, Marco, Tagaya, Mitsuo, Tai, Haoran, Tait, Stephen, Takahashi, Yoshinori, Takats, Szabolcs, Talwar, Priti, Tam, Chit, Tam, Shing Yau, Tampellini, Davide, Tamura, Atsushi, Tan, Chong Teik, Tan, Eng-King, Tan, Ya-Qin, Tanaka, Masaki, Tanaka, Motomasa, Tang, Daolin, Tang, Jingfeng, Tang, Tie-Shan, Tanida, Isei, Tao, Zhipeng, Taouis, Mohammed, Tatenhorst, Lars, Tavernarakis, Nektarios, Taylor, Allen, Taylor, Gregory, Taylor, Joan, Tchetina, Elena, Tee, Andrew, Tegeder, Irmgard, Teis, David, Teixeira, Natercia, Teixeira-Clerc, Fatima, Tekirdag, Kumsal, Tencomnao, Tewin, Tenreiro, Sandra, Tepikin, Alexei, Testillano, Pilar, Tettamanti, Gianluca, Tharaux, Pierre-Louis, Thedieck, Kathrin, Thekkinghat, Arvind, Thellung, Stefano, Thinwa, Josephine, Thirumalaikumar, V.P., Thomas, Sufi Mary, Thomes, Paul, Thorburn, Andrew, Thukral, Lipi, Thum, Thomas, Thumm, Michael, Tian, Ling, Tichy, Ales, Till, Andreas, Timmerman, Vincent, Titorenko, Vladimir, Todi, Sokol, Todorova, Krassimira, Toivonen, Janne, Tomaipitinca, Luana, Tomar, Dhanendra, Tomas-Zapico, Cristina, Tomić, Sergej, Tong, Benjamin Chun-Kit, Tong, Chao, Tong, Xin, Tooze, Sharon, Torgersen, Maria, Torii, Satoru, Torres-López, Liliana, Torriglia, Alicia, Towers, Christina, Towns, Roberto, Toyokuni, Shinya, Trajkovic, Vladimir, Tramontano, Donatella, Tran, Quynh-Giao, Travassos, Leonardo, Trelford, Charles, Tremel, Shirley, Trougakos, Ioannis, Tsao, Betty, Tschan, Mario, Tse, Hung-Fat, Tse, Tak Fu, Tsugawa, Hitoshi, Tsvetkov, Andrey, Tumbarello, David, Tumtas, Yasin, Tuñón, María, Turcotte, Sandra, Turk, Boris, Turk, Vito, Turner, Bradley, Tuxworth, Richard, Tyler, Jessica, Tyutereva, Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gomez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Alvarez, E. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. Y., Antas, P., Antebi, A., Anton, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araujo, W. L., Araya, J., Arden, C., Arevalo, M. -A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A. R., Armstrong-James, D., Arnaune-Pelloquin, L., Aroca, A., Arroyo, D. S., Arsov, I., Artero, R., Asaro, D. M. L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A. G., Au, A. K., Auberger, P., Auner, H. W., Aurelian, L., Autelli, R., Avagliano, L., Avalos, Y., Aveic, S., Aveleira, C. A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M., Backer, J. M., Backues, S. K., Bae, D. -H., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, A., Baek, S. -H., Baek, S. H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C. T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banreti, A., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barila, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touze, N., Bellarosa, C., Belleudi, F., Bello Perez, M., Bello-Morales, R., Beltran, J. S. D. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. 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S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A. M., Stupack, D. G., Su, H., Su, L. -Y., Su, L., Suarez-Fontes, A. M., Subauste, C. S., Subbian, S., Subirada, P. V., Sudhandiran, G., Sue, C. M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M. -X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K. K. S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J. D., Sze, S. C. W., Szewczyk, N. J., Tabecka-Lonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S. W. G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S. Y., Tampellini, D., Tamura, A., Tan, C. T., Tan, E. -K., Tan, Y. -Q., Tanaka, M., Tang, D., Tang, J., Tang, T. -S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G. A., Taylor, J. M., Tchetina, E., Tee, A. R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K. A., Tencomnao, T., Tenreiro, S., Tepikin, A. V., Testillano, P. S., Tettamanti, G., Tharaux, P. -L., Thedieck, K., Thekkinghat, A. A., Thellung, S., Thinwa, J. W., Thirumalaikumar, V. P., Thomas, S. M., Thomes, P. G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V. I., Todi, S. V., Todorova, K., Toivonen, J. M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomic, S., Tong, B. C. -K., Tong, C., Tong, X., Tooze, S. A., Torgersen, M. L., Torii, S., Torres-Lopez, L., Torriglia, A., Towers, C. G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q. -G., Travassos, L. H., Trelford, C. B., Tremel, S., Trougakos, I. P., Tsao, B. P., Tschan, M. P., Tse, H. -F., Tse, T. F., Tsugawa, H., Tsvetkov, A. S., Tumbarello, D. A., Tumtas, Y., Tunon, M. J., Turcotte, S., Turk, B., Turk, V., Turner, B. J., Tuxworth, R. I., Tyler, J. K., Tyutereva, E. V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H. H., Ulamek-Koziol, M., Ulasov, I. V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Ustun, S., Uversky, V. N., Vaccari, T., Vaccaro, M. I., Vahsen, B. F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M. J., Valko, A., Vallee, R. B., Valverde, A. M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S. J. L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M. A., Vannini, N., Vanrell, M. C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M. H., Vats, S., Vavvas, D. G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velazquez, A. P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A. T., Victor, V. M., Vidal, M., Vidoni, C., Vieira, O. V., Vierstra, R. D., Vigano, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J. M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M. T., Visnjic, D., Vitale, I., Vocadlo, D. J., Voitsekhovskaja, O. V., Volonte, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M. A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K. A., Wakatsuki, S., Walker, D. W., Walker, M. J., Walker, S. A., Walter, J., Wandosell, F. G., Wang, B., Wang, C. -Y., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, H. -G., Wang, J., Wang, K., Wang, L., Wang, M. H., Wang, M., Wang, N., Wang, P., Wang, Q. J., Wang, Q., Wang, Q. K., Wang, Q. A., Wang, W. -T., Wang, W., Wang, X., Wang, Y., Wang, Y. -Y., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzynska, A., Weaver, T. E., Wegrzyn, G., Wehman, A. M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergraber, O. H., Weihl, C. C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R. H., Wen, X., Werner, A., Weykopf, B., Wheatley, S. P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S. -J., Yan, Z., Yanagi, Y., Yang, C., Yang, D. -S., Yang, H., Yang, H. -T., Yang, J. -M., Yang, J., Yang, L., Yang, M., Yang, P. -M., Yang, Q., Yang, S., Yang, S. -F., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y. -G., Yao, Y. -M., Yasui, T., Yazdankhah, M., Yen, P. M., Yi, C., Yin, X. -M., Yin, Y., Yin, Z., Ying, M., Ying, Z., Yip, C. K., Yiu, S. P. T., Yoo, Y. H., Yoshida, K., Yoshii, S. R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, L., Yu, M. -L., Yu, S. -W., Yu, V. C., Yu, W. H., Yu, Z., Yuan, J., Yuan, L. -Q., Yuan, S., Yuan, S. -S. F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R. L., Zacks, D. N., Zaffagnini, G., Zambelli, V. O., Zanella, I., Zang, Q. S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K. S., Zarebkohan, A., Zarrouk, A., Zeitlin, S. O., Zeng, J., Zeng, J. -D., Zerovnik, E., Zhan, L., Zhang, B., Zhang, D. D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021
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17. Ribotoxin-like proteins from Boletus edulis: structural properties, cytotoxicity and in vitro digestibility

Author: Elio Pizzo, Rosita Russo, Rosanna Culurciello, Sara Ragucci, Mariangela Valletta, Antimo Di Maro, Nicola Landi, Paolo V. Pedone, Landi, N., Ragucci, S., Culurciello, R., Russo, R., Valletta, M., Pedone, P. V., Pizzo, E., and Di Maro, A.
Subjects: Protein Conformation, Proteolysis, Porcini, Fungal Protein, 01 natural sciences, Analytical Chemistry, Ribotoxin-like protein, Fungal Proteins, Ribonuclease, 0404 agricultural biotechnology, medicine, Humans, Ingestion, Food science, Mushroom poisoning, Ageritin, Toxins, Biological, chemistry.chemical_classification, Edible mushroom, Food poisoning, biology, medicine.diagnostic_test, business.industry, Chemistry, Basidiomycota, 010401 analytical chemistry, 04 agricultural and veterinary sciences, General Medicine, Food safety, biology.organism_classification, medicine.disease, 040401 food science, 0104 chemical sciences, Ribotoxin-like proteins, Protein purification, Enzyme, Boletus edulis, Toxicity, business, Food Science, Human
Abstract: Porcini are edible mushrooms widely used in cooking due to their extraordinary taste. Despite this, cases of food poisoning have been reported in the recent literature also for ingestion of porcini. Here, we report the isolation from Boletus edulis fruiting bodies of two novel ribotoxin-like proteins (RL-Ps), enzymes already studied in other organisms for their toxicity. These RL-Ps, named Edulitin 1 (16-kDa) and Edulitin 2 (14-kDa), show peculiar structural and enzymatic differences, which probably reflect their different bio-activities and a dose/time dependent toxicity (Edulitin 2) on normal and tumoral human cells. Particularly interesting is the resistance to proteolysis of Edulitin 2, for which it was observed that its toxicity was abolished only after heat treatment (90 °C) followed by proteolysis. As mushroom poisoning is a serious food safety issue, data here presented confirm the existence of toxins also in porcini and the importance of a proper cooking before their consumption.
Published: 2021

18. Calcium Signaling and Mitochondrial Function in Presenilin 2 Knock-Out Mice: Looking for Any Loss-of-Function Phenotype Related to Alzheimer’s Disease

Author: Mauro Giacca, Alice Rossi, Luisa Galla, Valentina Giorgio, Chiara Gomiero, Lorena Zentilin, Tullio Pozzan, Tito Calì, Paola Pizzo, Elisa Greotti, Rossi, Alice, Galla, Luisa, Gomiero, Chiara, Zentilin, Lorena, Giacca, Mauro, Giorgio, Valentina, Calì, Tito, Pozzan, Tullio, Greotti, Elisa, and Pizzo, Paola
Subjects: Amyloid beta, Cell Respiration, Citric Acid Cycle, PS2–/–, Mitochondrion, Biology, bioenergetics, Endoplasmic Reticulum, Presenilin, Article, Oxidative Phosphorylation, 03 medical and health sciences, 0302 clinical medicine, presenilin 2, mitochondrial membrane potential, Adenosine Triphosphate, Cytosol, Ca2+ signaling, Alzheimer Disease, PSEN2, Presenilin-2, PSEN1, Amyloid precursor protein, Animals, Calcium Signaling, skin and connective tissue diseases, lcsh:QH301-705.5, Loss function, 030304 developmental biology, Calcium signaling, Membrane Potential, Mitochondrial, Mice, Knockout, Neurons, 0303 health sciences, bioenergetic, General Medicine, Cell biology, neuronal hyperexcitability, Mitochondria, Mice, Inbred C57BL, Alzheimer′s disease, Phenotype, lcsh:Biology (General), oxygen consumption rate, biology.protein, Glycolysis, 030217 neurology & neurosurgery
Abstract: Alzheimer&prime, s disease (AD) is the most common age-related neurodegenerative disorder in which learning, memory and cognitive functions decline progressively. Familial forms of AD (FAD) are caused by mutations in amyloid precursor protein (APP), presenilin 1 (PSEN1) and presenilin 2 (PSEN2) genes. Presenilin 1 (PS1) and its homologue, presenilin 2 (PS2), represent, alternatively, the catalytic core of the &gamma, secretase complex that, by cleaving APP, produces neurotoxic amyloid beta (A&beta, ) peptides responsible for one of the histopathological hallmarks in AD brains, the amyloid plaques. Recently, PSEN1 FAD mutations have been associated with a loss-of-function phenotype. To investigate whether this finding can also be extended to PSEN2 FAD mutations, we studied two processes known to be modulated by PS2 and altered by FAD mutations: Ca2+ signaling and mitochondrial function. By exploiting neurons derived from a PSEN2 knock-out (PS2&ndash, /&ndash, ) mouse model, we found that, upon IP3-generating stimulation, cytosolic Ca2+ handling is not altered, compared to wild-type cells, while mitochondrial Ca2+ uptake is strongly compromised. Accordingly, PS2&ndash, neurons show a marked reduction in endoplasmic reticulum&ndash, mitochondria apposition and a slight alteration in mitochondrial respiration, whereas mitochondrial membrane potential, and organelle morphology and number appear unchanged. Thus, although some alterations in mitochondrial function appear to be shared between PS2&ndash, and FAD-PS2-expressing neurons, the mechanisms leading to these defects are quite distinct between the two models. Taken together, our data appear to be difficult to reconcile with the proposal that FAD-PS2 mutants are loss-of-function, whereas the concept that PS2 plays a key role in sustaining mitochondrial function is here confirmed.
Published: 2021

19. Long-standing multiple system atrophy-Parkinsonism with limbic and FTLD-type α-synuclein pathology

Author: Vanessa Goodwill, Brenton A Wright, Annie Hiniker, Donald P. Pizzo, Ian Dryden, Douglas Galasko, Ian R. A. Mackenzie, David G. Coughlin, and Stephanie Lessig
Subjects: Pathology, medicine.medical_specialty, Histology, Synucleinopathies, Cytoplasmic inclusion, Autopsy, Biology, Article, Pathology and Forensic Medicine, White matter, Atrophy, Parkinsonian Disorders, Physiology (medical), mental disorders, medicine, Humans, Parkinsonism, Multiple System Atrophy, medicine.disease, nervous system diseases, medicine.anatomical_structure, nervous system, Neurology, Gliosis, alpha-Synuclein, Immunohistochemistry, Neurology (clinical), Age of onset, medicine.symptom, Frontotemporal Lobar Degeneration
Abstract: Multiple system atrophy (MSA) is a sporadic neurodegenerative disease clinically marked by autonomic failure and variable degrees of parkinsonism and cerebellar ataxias. The average age of onset is in the sixth decade of life with a five-year survival, although fulminant and more benign courses have been described (1). The pathologic hallmark of MSA is abundant α-synuclein-positive protein aggregates within oligodendrocytes (glial cytoplasmic inclusions, GCI) and neurons (neuronal cytoplasmic inclusions, NCI, and neuronal nuclear inclusions, NNI). The density of GCIs has been correlated with disease duration and severity of neuronal loss (2). Here, we present an unusual case of MSA clinically characterized by rapid decline followed by a 20-year disease duration in a severely affected state. At autopsy, the brain showed severe gliosis and neuronal loss in a pattern characteristic of MSA. Additionally, there were atypical Pick body-like and ring-shaped α-synuclein inclusions, most prominent in limbic regions, consistent with a recently described subtype of MSA designated "atypical MSA" (3). Four different α-synuclein antibodies highlighted only scant α-synuclein-positive pathology; however, Gallyas and Campbell-Switzer silver stains identified additional GCIs most prominent in subcortical white matter. Interestingly, many of the α-synuclein-positive limbic inclusions were Gallyas-negative, while many of the Gallyas-positive inclusions were α-synuclein-negative (4). This observation of markedly disparate α-synuclein immunohistochemical versus Gallyas reactivity of MSA inclusions is unusual and could support the possibility that MSA inclusions have variable compositions, something which has been recently suggested (5).
Published: 2021

20. Agritourism and Kidding Season: A Large Outbreak of Human Shiga Toxin-Producing Escherichia coli O157 (STEC O157) Infections Linked to a Goat Dairy Farm—Connecticut, 2016

Author: Paul Gacek, Anthony Muyombwe, Matthew L. Cartter, Jafar Razeq, Mary Jane Lis, Lauren M. Gollarza, Morgan N Schroeder, Nancy Strockbine, Tu Ngoc Nguyen, Eshaw Vidyaprakash, Bruce Sherman, Mark E. Laughlin, Kelly Gambino-Shirley, Eugene Pizzo, Quyen Phan, Alexandra Mercante, Patrick McCormack, Haley Martin, Anna J. Blackstock, Samantha M. Olson, Alycia McNutt, Jocelyn Mullins, Laura Whitlock, Kimberly Holmes-Talbot, Megin Nichols, Wayne Kasacek, Diane Noel, and Laurn Mank
Subjects: medicine.medical_specialty, Veterinary medicine, E. coli–Escherichia coli, animal diseases, diarrhea, Biology, Serology, fluids and secretions, Hand sanitizer, children, SF600-1100, medicine, Feces, Original Research, outbreak, General Veterinary, Public health, goat, Shiga toxin (Stx) producing Escherichia coli (STEC), agritourism, Outbreak, Diarrhea, hemolytic uremic syndrome, Hay, Veterinary Science, medicine.symptom, Barn (unit)
Abstract: The objective of this study was to determine sources of Shiga toxin-producing Escherichia coli O157 (STEC O157) infection among visitors to Farm X and develop public health recommendations. A case-control study was conducted. Case-patients were defined as the first ill child (aged ; of these, 62% (18 of 29) yielded STEC O157 highly related by WGS to patient isolates. STEC O157 environmental contamination and fecal shedding by goats at Farm X was extensive. Farms should provide handwashing stations with soap, running water, and disposable towels. Access to animal areas, including animal pens and enclosures, should be limited for young children who are at risk for severe outcomes from STEC O157 infection. National recommendations should be adopted to reduce disease transmission.
Published: 2021
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21. In Vitro Anti-Epstein Barr Virus Activity of Olea europaea L. Leaf Extracts

Author: Hamadi Attia, Ichrak Ben-Amor, Imen Kallel, Maria Musarra-Pizzo, Rosamaria Pennisi, Bochra Gargouri, Khaoula Tlili, and Maria Teresa Sciortino
Subjects: Antioxidant, antioxidant, Ecology, biology, Chemistry, DPPH, medicine.medical_treatment, Botany, Plant Science, biology.organism_classification, Molecular biology, In vitro, Raji cell, Lipid peroxidation, chemistry.chemical_compound, antivirals, Lipid oxidation, Lytic cycle, Olea, QK1-989, medicine, Olea europaea leaves, Ecology, Evolution, Behavior and Systematics, plants bioactive compounds
Abstract: Olea europaea L. var. sativa (OESA) preparations are widely used in traditional medicine in the Mediterranean region to prevent and treat different diseases. In this research, olive extracts derived from the leaves of the OESA tree have been screened for antioxidant activity by two methods: the DPPH free radical scavenging assay (DPPH) and the Ferric reducing antioxidant power (FRAP) assay. The DPPH assay showed that OESA possesses a stronger antioxidant activity (84%) at 1 mg/mL while the FRAP method showed a strong metal ion chelating activity (90%) at 1 mg/mL. The low IC50 values, obtained by two different methods, implies that OESA has a noticeable effect on scavenging free radicals comparable to standards. During EBV infection, the free radicals increased triggering lipid oxidation. Therefore, the monitoring of the secondary lipid peroxidation products was done by measuring malonaldehyde (MDA) and conjugated dienes (DC). The simultaneous treatment of Raji cells with OESA and TPA, as an inductorof the lytic cycle, generated a significant decrease in MDA levels and DC (p &lt, 0.05). Besides, Raji cells simultaneously exposed to TPA and OESA exhibited a percentage of EBV-positive fluorescence cells lower than TPA treated cells (**** p &lt, 0.0001). This suggests that OESA treatment has a protective effect against EBV lytic cycle induction.
Published: 2021
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22. Assessment of the feed additive consisting of sodium benzoate (Protural®) for weaned piglets for the renewal of its authorisation and the extension of use to other growing Suidae (Taminco Finland Oy)

Author: Giovanna Azimonti, Yolanda Sanz, Vasileios Bampidis, Secundino López Puente, Henrik Christensen, Baltasar Mayo, Maria de Lourdes Bastos, Mojca Fašmon Durjava, Fabiola Pizzo, Maryline Kouba, Efsa Panel on Additives, Jaume Galobart, Mariana Petkova, Montserrat Anguita, Birgit Dusemund, Marta López-Alonso, Alena Pechová, Ruud Woutersen, Fernando Ramos, Roberto Edoardo Villa, and Francesca Marcon
Subjects: Protural, Animal feed, Veterinary (miscellaneous), Feed additive, sodium benzoate, Context (language use), TP1-1185, Plant Science, Microbiology, Anim2953, chemistry.chemical_compound, Animal science, Weaned piglets, Suidae, other growing Suidae, Medicine, TX341-641, European commission, weaned piglets, renewal, extension of use, biology, Nutrition. Foods and food supply, business.industry, Chemical technology, Authorization, biology.organism_classification, Scientific Opinion, chemistry, Sodium benzoate, Animal Science and Zoology, Parasitology, business, Food Science
Abstract: Following a request from the European Commission, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of Protural® (sodium benzoate) when used as a zootechnical additive in feed for weaned piglets and other growing Suidae at 4,000 mg/kg feedingstuff. Protural® consists of sodium benzoate without any carrier materials and is currently authorised for use in weaned piglets. This opinion concerns the renewal of the authorisation of Protural® for weaned piglets and the evaluation of the new use in other growing Suidae. The applicant provided evidence that the additive currently in the market complies with the existing conditions of authorisation. The FEEDAP Panel concluded that Protural® is safe under the current conditions of authorisation for the target species, consumers of products from animals fed the additive and the environment. Protural® was not considered as irritant to skin and eyes but a skin sensitiser. Based on dusting potential data, the FEEDAP Panel considered that the powder formulation of the additive represented a risk by inhalation. There was no need for assessing the efficacy of Protural® in the context of the renewal of the authorisation for weaned piglets. The efficacy data previously evaluated allowed the FEEDAP Panel to conclude that the additive has the potential to be efficacious at the level of 4,000 mg/kg feedingstuff in other growing Suidae. A conclusion cannot be reached for the efficacy in pigs for fattening.
Published: 2021

23. Safety and efficacy of a feed additive consisting of 3‐nitrooxypropanol (Bovaer® 10) for ruminants for milk production and reproduction (DSM Nutritional Products Ltd)

Author: Henrik Christensen, Mojca Fašmon Durjava, Jürgen Gropp, Fernando Ramos, Vasileios Bampidis, Birgit Dusemund, Maria de Lourdes Bastos, Baltasar Mayo, Maryline Kouba, Yolanda Sanz, Giovanna Azimonti, Kettil Svensson, Paul Brantom, Paola Manini, Roberto Edoardo Villa, Secundino López Puente, Francesca Marcon, Gabriele Aquilina, Efsa Panel on Additives, Ruud Woutersen, Jaume Galobart, Mariana Petkova, Montserrat Anguita, Luca Tosti, Georges Bories, Marta López-Alonso, Fabiola Pizzo, Alena Pechová, and Jordi Tarrés-Call
Subjects: Settore VET/07 - Farmacologia e Tossicologia Veterinaria, Veterinary (miscellaneous), media_common.quotation_subject, Feed additive, Nutritional products, Plant Science, TP1-1185, Biology, 3‐NOP, 3‐nitrooxypropanol, 3‐nitrooxypropionic acid, NOPA, environment, methane reduction, ruminants, zootechnical additive, Microbiology, Settore MED/44 - Medicina del Lavoro, 3-nitrooxypropanol, TX341-641, Food science, media_common, Nutrition. Foods and food supply, Chemical technology, Milk production, Animal Science and Zoology, Parasitology, Reproduction, Food Science
Abstract: Following a request from the European Commission, EFSA was asked to deliver a scientific opinion on the safety and efficacy of Bovaer® 10 as a zootechnical additive for ruminants for milk production and reproduction. Systemic exposure or site of contact toxicity for the active substance 3‐nitrooxypropanol (3‐NOP), for which genotoxicity has not been fully clarified, in the target species, is unlikely based on ADME data available. Consequently, the FEEDAP Panel concluded that Bovaer® 10 was safe for dairy cows at the maximum recommended level. However, as a margin of safety could not be established, the FEEDAP Panel could not conclude on the safety of the additive for other animal species/categories. The FEEDAP Panel considered that the consumer was exposed to 3‐nitrooxypropionic acid (NOPA), which is one of the 3‐NOP metabolites. NOPA was not genotoxic based on the studies provided. The FEEDAP Panel concluded that the use of Bovaer® 10 in animal nutrition under the conditions of use proposed was of no concern for consumer safety and for the environment. The FEEDAP Panel concluded that the active substance 3‐NOP may be harmful if inhaled. It is irritant (but not corrosive) to skin, irritant to the eyes but it is not a skin sensitiser. As the genotoxicity of 3‐NOP is not completely elucidated, the exposure through inhalation of the additive may represent an additional risk for the user. The Panel concluded that the additive has a potential to be efficacious in dairy cows to reduce enteric methane production under the proposed conditions of use. This conclusion was extrapolated to all other ruminants for milk production and reproduction.
Published: 2021

24. Safety of 3-phytase FLF1000 and FSF10000 as a feed additive for pigs for fattening and minor growing porcine species

Author: Elisa Pettenati, Paola Manini, Giovanna Azimonti, Henrik Christensen, Efsa Panel on Additives, Birgit Dusemund, Jaume Galobart, Secundino López Puente, Baltasar Mayo, Noël Dierick, Montserrat Anguita, Roberto Edoardo Villa, Vasileios Bampidis, Mariana Petkova, Alena Pechová, Fabiola Pizzo, Yolanda Sanz, Mojca Kos Durjava, Orsolya Holczknecht, Marta López-Alonso, Ruud Woutersen, Giovanna Martelli, Jordi Tarrés-Call, Maria de Lourdes Bastos, Maryline Kouba, Fernando Ramos, Francesca Marcon, Bampidis V., Azimonti G., Bastos M.D.L., Christensen H., Dusemund B., Kouba M., Kos Durjava M., Lopez-Alonso M., Lopez Puente S., Marcon F., Mayo B., Pechova A., Petkova M., Ramos F., Sanz Y., Villa R.E., Woutersen R., Dierick N.A., Martelli G., Galobart J., Holczknecht O., Manini P., Pettenati E., Pizzo F., Tarres-Call J., and Anguita M.
Subjects: pig, safety, Veterinary (miscellaneous), Feed additive, 3-phytase, efficacy, TP1-1185, Plant Science, Biology, Microbiology, Porcine species, TX341-641, Food science, digestibility enhancers, Nutrition. Foods and food supply, Chemical technology, pigs, 3‐phytase, Scientific Opinion, Zootechnical additive, Animal Science and Zoology, Parasitology, Phytase, substances which favourably affect the environment, digestibility enhancer, Food Science
Abstract: Following a request from the European Commission, the Panelon Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety of 3-phytase FLF1000/FSF10000 as a feed additive for pigs for fattening and minor porcine species for growing. This additive contains 3-phytase produced by a genetically modified strain of Komagataella phaffii and it is authorised in its liquid FLF1000 and solid form FSF10000 as a feed additive for chickens for fattening, laying hens, chickens reared for laying and for minor poultry species for fattening or reared for laying or for breeding. The FEEDAP Panelhas adopted an opinion regarding the use of this product as a feed additive in pigs for fattening and minor porcine species for growing. In that opinion, the FEEDAP Panelconcluded that the use of the product as a feed additive would raise no concerns for the consumer safety nor for the environment but that the additive should be regarded as a potential respiratory sensitizer. The Panelalso concluded that the additive has a potential to be efficacious in improving the phosphorus utilisation in the target species. However, the Panelcould not conclude on the safety for the target species due to the limitations identified in the data provided. The applicant has now complemented the information and made it available to the Panel. The tolerance trial was done in weaned piglets in which the animals received up to 10 times the recommended dose of 1,000 FTU/kg feed. The results showed no adverse effects of the phytase on the performance of the animals or on the haematological and biochemical parameters measured in blood. Therefore, the Panelconcluded that the additive (3-phytase FLF1000 and FSF10000) is safe for pigs for fattening and minor growing porcine species at the recommended dose of 1,000 FTU/kg feed.
Published: 2020

25. Safety and efficacy of Axtra® XAP 104 TPT (endo‐1,4‐xylanase, protease and alpha‐amylase) as a feed additive for chickens for fattening, laying hens and minor poultry species

Author: Secundino López Puente, Mojca Kos Durjava, Elisa Pettenati, Yolanda Sanz, Giovanna Martelli, Luca Tosti, Pier Sandro Cocconcelli, Kettil Svensson, Birgit Dusemund, Fabiola Pizzo, Maria de Lourdes Bastos, Maryline Kouba, Noël Dierick, Lieve Herman, Jaume Galobart, Boet Glandorf, Henrik Christensen, Francesca Marcon, Roberto Edoardo Villa, Mariana Petkova, Miguel Prieto Maradona, Vasileios Bampidis, Marta López-Alonso, Giovanna Azimonti, Montserrat Anguita, Fernando Ramos, Alena Pechová, Efsa Panel on Additives, Maria Saarela, Ruud Woutersen, Baltasar Mayo, Bampidis V., Azimonti G., Bastos M.D.L., Christensen H., Dusemund B., Kos Durjava M., Kouba M., Lopez-Alonso M., Lopez Puente S., Marcon F., Mayo B., Pechova A., Petkova M., Ramos F., Sanz Y., Villa R.E., Woutersen R., Cocconcelli P.S., Dierick N.A., Glandorf B., Herman L., Prieto Maradona M., Martelli G., Tosti L., Saarela M., Svensson K., Galobart J., Pettenati E., Pizzo F., and Anguita M.
Subjects: safety, Veterinary (miscellaneous), medicine.medical_treatment, Feed additive, efficacy, Plant Science, TP1-1185, Microbiology, medicine, TX341-641, Food science, digestibility enhancers, xylanase, Protease, biology, Chemistry, Nutrition. Foods and food supply, poultry, Chemical technology, alpha-amylase, protease, zootechnical additives, Xylanase, biology.protein, Animal Science and Zoology, Parasitology, Alpha-amylase, Food Science, digestibility enhancer
Abstract: Following a request from the European Commission, the EFSA Panelon Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy ofAxtra® XAP 104 TPT as a zootechnical feed additive (digestibility enhancers) for poultry species. The additive contains three enzyme activities (endo-1,4-beta-xylanase, protease and alpha-amylase) produced by three different genetically modified strains. Viable cells and recombinant DNA of the strains producing the protease and amylase were not detected in the final product. Owing to the insufficient data, uncertainty remained on the presence in the additive of viable cells of the strain producing the xylanase. The results obtained in the genotoxicity and subchronic oral toxicity studies performed with the three fermentation products did not indicate safety concerns resulting from the fermentation products used in the formulation/manufacturing. However, uncertainties remain on the suitability of the test item used in the studies conducted with the xylanase; therefore, the Panelwas not in the position to conclude on the toxicological potential of AXTRA® XAP 104 TPT. Consequently, the Panelcould not conclude on the safety of the additive for the target species, consumers and users. Owing to the uncertainty on the presence of viable cells of one of the production strains in the additive, the Panelcould not conclude on the safety for the environment. The FEEDAP Panelconcluded that AXTRA® XAP 104 TPT is efficacious in chickens for fattening, chickens reared for laying and minor poultry species up to the point of lay at the level of 2,000 U xylanase, 200 U amylase and 4,000 U protease per kg feed. Owing to the lack of sufficient data, the Panelcould not conclude on the efficacy of the additive for laying hens.
Published: 2020

26. Cryptides Identified in Human Apolipoprotein B as New Weapons to Fight Antibiotic Resistance in Cystic Fibrosis Disease

Author: Rosa Gaglione, Elio Pizzo, Eliana Dell’Olmo, Luca Tartaglione, Rocco Di Girolamo, Angela Arciello, Angela Cesaro, Gaglione, Rosa, Cesaro, Angela, Dell’Olmo, Eliana, DI GIROLAMO, Rocco, Tartaglione, Luca, Pizzo, Eliodoro, and Arciello, Angela
Subjects: 0301 basic medicine, antibiotic resistance, antimicrobial peptide, Cystic Fibrosis, Antibiotics, Cystic fibrosis, lcsh:Chemistry, antimicrobial peptides, lcsh:QH301-705.5, Spectroscopy, biology, cryptide, host defense peptides, Drug Synergism, General Medicine, Bacterial Infections, Antimicrobial, Computer Science Applications, Anti-Bacterial Agents, Ciprofloxacin, Host-Pathogen Interactions, Pseudomonas aeruginosa, anti-biofilm peptide, synergistic effects, cryptides, medicine.drug, medicine.drug_class, 030106 microbiology, Antimicrobial peptides, Microbial Sensitivity Tests, Opportunistic Infections, Catalysis, Article, anti-biofilm peptides, Microbiology, Inorganic Chemistry, 03 medical and health sciences, Antibiotic resistance, Drug Resistance, Bacterial, medicine, host defense peptide, Humans, Pseudomonas Infections, Physical and Theoretical Chemistry, Molecular Biology, cystic fibrosi, Apolipoproteins B, business.industry, Organic Chemistry, biology.organism_classification, medicine.disease, Multiple drug resistance, 030104 developmental biology, Burkholderia, lcsh:Biology (General), lcsh:QD1-999, Biofilms, business, Antimicrobial Cationic Peptides
Abstract: Chronic respiratory infections are the main cause of morbidity and mortality in cystic fibrosis (CF) patients, and are characterized by the development of multidrug resistance (MDR) phenotype and biofilm formation, generally recalcitrant to treatment with conventional antibiotics. Hence, novel effective strategies are urgently needed. Antimicrobial peptides represent new promising therapeutic agents. Here, we analyze for the first time the efficacy of three versions of a cryptide identified in human apolipoprotein B (ApoB, residues 887-922) towards bacterial strains clinically isolated from CF patients. Antimicrobial and anti-biofilm properties of ApoB-derived cryptides have been analyzed by broth microdilution assays, crystal violet assays, confocal laser scanning microscopy and scanning electron microscopy. Cell proliferation assays have been performed to test cryptide effects on human host cells. ApoB-derived cryptides have been found to be endowed with significant antimicrobial and anti-biofilm properties towards Pseudomonas and Burkholderia strains clinically isolated from CF patients. Peptides have been also found to be able to act in combination with the antibiotic ciprofloxacin, and they are harmless when tested on human bronchial epithelial mesothelial cells. These findings open interesting perspectives to cryptide applicability in the treatment of chronic lung infections associated with CF disease.
Published: 2020

27. Defective Mitochondrial Pyruvate Flux Affects Cell Bioenergetics in Alzheimer's Disease-Related Models

Author: Alice Rossi, Paola Pizzo, Riccardo Filadi, Giulia Rigotto, Valentina Giorgio, Giulia Valente, Emy Basso, Rossi A., Rigotto G., Valente G., Giorgio V., Basso E., Filadi R., and Pizzo P.
Subjects: 0301 basic medicine, Pyruvate decarboxylation, mitochondrial metabolism, Bioenergetics, Alzheimer's disease, bioenergetics, calcium homeostasis, GSK-3b, hexokinase 1, mitochondrial pyruvate carrier, presenilin, pyruvate, calcium homeostasi, Cell, Excitotoxicity, Mitochondrion, medicine.disease_cause, Transfection, General Biochemistry, Genetics and Molecular Biology, Presenilin, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Alzheimer Disease, Pyruvic Acid, medicine, Animals, Humans, lcsh:QH301-705.5, Hexokinase, ATP synthase, biology, bioenergetic, Cell biology, Mitochondria, Disease Models, Animal, 030104 developmental biology, medicine.anatomical_structure, lcsh:Biology (General), chemistry, biology.protein, Energy Metabolism, 030217 neurology & neurosurgery
Abstract: Summary: Mitochondria are key organelles for brain health. Mitochondrial alterations have been reported in several neurodegenerative disorders, including Alzheimer’s disease (AD), and the comprehension of the underlying mechanisms appears crucial to understand their relationship with the pathology. Using multiple genetic, pharmacological, imaging, and biochemical approaches, we demonstrate that, in different familial AD cell models, mitochondrial ATP synthesis is affected. The defect depends on reduced mitochondrial pyruvate oxidation, due to both lower Ca2+-mediated stimulation of the Krebs cycle and dampened mitochondrial pyruvate uptake. Importantly, this latter event is linked to glycogen-synthase-kinase-3β (GSK-3β) hyper-activation, leading, in turn, to impaired recruitment of hexokinase 1 (HK1) to mitochondria, destabilization of mitochondrial-pyruvate-carrier (MPC) complexes, and decreased MPC2 protein levels. Remarkably, pharmacological GSK-3β inhibition in AD cells rescues MPC2 expression and improves mitochondrial ATP synthesis and respiration. The defective mitochondrial bioenergetics influences glutamate-induced neuronal excitotoxicity, thus representing a possible target for future therapeutic interventions. : Mitochondria are key organelles for brain health. Rossi et al. show that, in different Alzheimer’s disease cell models, lower mitochondrial Ca2+ signal and pyruvate uptake reduce ATP synthesis. GSK-3β hyper-activation contributes to the defect by impairing HK1-mitochondria association, decreasing MPC2 levels and destabilizing MPC complexes. Defective bioenergetics affects neuronal functionality. Keywords: Alzheimer’s disease, presenilin, mitochondrial metabolism, bioenergetics, calcium homeostasis, pyruvate, mitochondrial pyruvate carrier, hexokinase 1, GSK-3b
Published: 2020

28. Safety and efficacy of OptiPhos® PLUS for suckling and weaned piglets, pigs for fattening, sows, other minor pig species for fattening and other minor reproductive pig species

Author: Yolanda Sanz, Efsa Panel on Additives, Roberto Edoardo Villa, Marta López-Alonso, Elisa Pettenati, Jordi Tarrés-Call, Montserrat Anguita, Paola Manini, Secundino López Puente, Vasileios Bampidis, Birgit Dusemund, Fabiola Pizzo, Alena Pechová, Noël Dierick, Giovanna Martelli, Mariana Petkova, Henrik Christensen, Giovanna Azimonti, Mojca Kos Durjava, Jaume Galobart, Maria de Lourdes Bastos, Ruud Woutersen, Maryline Kouba, Orsolya Holczknecht, Francesca Marcon, Fernando Ramos, Baltasar Mayo, Bampidis V., Azimonti G., Bastos M.D.L., Christensen H., Dusemund B., Kos Durjava M., Kouba M., Lopez-Alonso M., Lopez Puente S., Marcon F., Mayo B., Pechova A., Petkova M., Ramos F., Sanz Y., Villa R.E., Woutersen R., Dierick N.A., Martelli G., Anguita M., Galobart J., Holczknecht O., Manini P., Pettenati E., Tarres-Call J., and Pizzo F.
Subjects: OptiPhosPLUS, safety, 040301 veterinary sciences, Animal feed, Veterinary (miscellaneous), Feed additive, animal diseases, efficacy, sows, Context (language use), Plant Science, TP1-1185, 010501 environmental sciences, Biology, ®, 01 natural sciences, Microbiology, 0403 veterinary science, Animal science, Weaned piglets, TX341-641, 0105 earth and related environmental sciences, Komagataella phaffii, Nutrition. Foods and food supply, Chemical technology, OptiPhosPLUS®, pigs for fattening, Eye irritation, 04 agricultural and veterinary sciences, Genetically modified organism, Scientific Opinion, Margin of safety, Animal Science and Zoology, Parasitology, Food Science
Abstract: Following a request from the European Commission, the EFSA Panelon Additives and products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of OptiPhos® PLUS (6-phytase) as a zootechnical feed additive for suckling and weaned piglets, pigs for fattening, sows, other minor pig species for fattening and other minor reproductive pig species. The additive is a preparation of 6-phytase produced by a genetically modified strain of Komagataella phaffii and has been previously assessed by the FEEDAP Panelin the context of two applications for its use in different species/categories. The Panelconcluded in those opinions that the production strain is safe, and that the use of the additive as a feed additive would raise no safety concerns for the consumers and the environment. The additive was also considered not to be skin irritant but was found to be a dermal sensitiser. The FEEDAP Panelcould not conclude on the eye irritation potential of the additive. Owing to the proteinaceous nature of the active substance, the additive is considered a respiratory sensitiser. Based on the tolerance studies provided, the Panelconcluded that the additive is safe for the target species under the conditions of use with a wide margin of safety and therefore the conclusion were extended to suckling piglets and extrapolated to other minor pig species for fattening and to other minor reproductive pig species. The FEEDAP Panelconcluded that the additive has the potential to be efficacious in weaned piglets, pigs for fattening and in sows at the level of 250 FTU/kg feed and this conclusion were extended to suckling piglets and extrapolated to other minor pig species for fattening and to other minor reproductive pig species.
Published: 2020

29. Clinical and genetic analysis of a european cohort with pericentral retinitis pigmentosa

Author: Francesco Musacchia, Raffaella Brunetti-Pierri, Francesca Simonelli, Francesco Testa, Maria Rosaria Barillari, Mariateresa Pizzo, Marianthi Karali, Luigi D'Angelo, Paolo Melillo, Valentina Di Iorio, Sandro Banfi, Annalaura Torella, Karali, M., Testa, F., Brunetti Pierri, R., Di Iorio, V, Pizzo, M., Melillo, P., Barillari, M. R., Torella, A., Musacchia, F., D'Angelo, L., Banfi, S., and Simonelli, F.
Subjects: 0301 basic medicine, Male, Disease, Genetic analysis, USH2A, Cohort Studies, 0302 clinical medicine, Exome, Child, Spectroscopy, Genetics, Aged, 80 and over, General Medicine, Middle Aged, Phenotype, Computer Science Applications, Pedigree, Italy, Cohort, Female, Retinitis Pigmentosa, Retinopathy, Human, Adult, Adolescent, inherited retinal dystrophies, Biology, Article, Catalysis, Inorganic Chemistry, 03 medical and health sciences, Young Adult, Atrophy, Next generation sequencing, Retinitis pigmentosa, medicine, Humans, Genetic Testing, Physical and Theoretical Chemistry, Inherited retinal dystrophie, Molecular Biology, Aged, Organic Chemistry, medicine.disease, Pericentral retinitis pigmentosa, 030104 developmental biology, 030221 ophthalmology & optometry, Cohort Studie
Abstract: Retinitis pigmentosa (RP) is a clinically heterogenous disease that comprises a wide range of phenotypic and genetic subtypes. Pericentral RP is an atypical form of RP characterized by bone-spicule pigmentation and/or atrophy confined in the near mid-periphery of the retina. In contrast to classic RP, the far periphery is better preserved in pericentral RP. The aim of this study was to perform the first detailed clinical and genetic analysis of a cohort of European subjects with pericentral RP to determine the phenotypic features and the genetic bases of the disease. A total of 54 subjects from 48 independent families with pericentral RP, non-syndromic and syndromic, were evaluated through a full ophthalmological examination and underwent clinical exome or retinopathy gene panel sequencing. Disease-causative variants were identified in 22 of the 35 families (63%) in 10 different genes, four of which are also responsible for syndromic RP. Thirteen of the 34 likely pathogenic variants were novel. Intra-familiar variability was also observed. The current study confirms the mild phenotype of pericentral RP and extends the spectrum of genes associated with this condition. Retinitis pigmentosa (RP) is a clinically heterogenous disease that comprises a wide range of phenotypic and genetic subtypes. Pericentral RP is an atypical form of RP characterized by bone-spicule pigmentation and/or atrophy confined in the near mid-periphery of the retina. In contrast to classic RP, the far periphery is better preserved in pericentral RP. The aim of this study was to perform the first detailed clinical and genetic analysis of a cohort of European subjects with pericentral RP to determine the phenotypic features and the genetic bases of the disease. A total of 54 subjects from 48 independent families with pericentral RP, non-syndromic and syndromic, were evaluated through a full ophthalmological examination and underwent clinical exome or retinopathy gene panel sequencing. Disease-causative variants were identified in 22 of the 35 families (63%) in 10 different genes, four of which are also responsible for syndromic RP. Thirteen of the 34 likely pathogenic variants were novel. Intra-familiar variability was also observed. The current study confirms the mild phenotype of pericentral RP and extends the spectrum of genes associated with this condition.
Published: 2020

30. Characterisation of EFV12 a bio-active small peptide produced by the human intestinal isolate Lactobacillus gasseri SF1109

Author: Andrea Carpentieri, Gerardino D'Errico, Anna Zanfardino, Giuseppe Vitiello, B Di Luccia, Eliodoro Pizzo, Mario Varcamonti, Alessandro Pezzella, M. Di Napoli, Eugenio Notomista, Di Napoli, M., Di Luccia, B., Vitiello, G., D'Errico, G., Carpentieri, A., Pezzella, A., Pizzo, E., Notomista, E., Varcamonti, M., and Zanfardino, A.
Subjects: 0301 basic medicine, Microbiology (medical), p38 mitogen-activated protein kinases, Lactobacillus gasseri, 01 natural sciences, Microbiology, law.invention, 03 medical and health sciences, Probiotic, law, medicine, Extracellular, Receptor, biology, 010405 organic chemistry, Kinase, Chemistry, Antimicrobial, biology.organism_classification, 0104 chemical sciences, 030104 developmental biology, Mechanism of action, Biochemistry, medicine.symptom, LPS binding, Antimicrobial peptide
Abstract: EFV12 is a small bioactive peptide produced by Lactobacillus gasseri SF1109, a human intestinal isolate with probiotic features. In this study, EFV12 antimicrobial and anti-inflammatory properties are characterised. In particular, we propose a possible mechanism of action for EFV12 involving bacterial membranes targeting. Moreover, we show that this small peptide is able to bind lipopolysaccharides (LPS) and to counteract its inflammatory insult preventing LPS action on Toll-like receptor 4, thus interfering with extracellular signal-regulated kinase, p38 and Jun N-terminal kinase, mitogen-activated protein kinases signalling pathways. Altogether these observations suggest that the bioactive peptide EFV12 is a good candidate to promote L. gasseri induced gut homeostasis and counteracting intestinal pathogens.
Published: 2020

31. GVF27, a human derived peptide with anti-infective properties against biofilm forming members of the Burkholderia cepacia complex

Author: Eugenio Notomista, Rosanna Culurciello, Valeria Cafaro, Elio Pizzo, Rocco Di Girolamo, Angela Arciello, Andrea Bosso, Salvatore Fusco, Edwin J.A. Veldhuizen, Rosa Gaglione, and Pilar García-Vello
Subjects: chemistry.chemical_classification, Burkholderia cepacia complex, chemistry, biology, Biofilm, Anti infectives, Peptide, biology.organism_classification, Microbiology
Abstract: Therapeutic solutions to counter Burkholderia cepacia complex (Bcc) bacteria are challenging due to their intrinsically high level of antibiotic resistance. Bcc organisms display a variety of potential virulence factors, have a distinct lipopolysaccharide naturally implicated in antimicrobial resistance and are able to form biofilms, which may further protect them from both host defence peptides (HDPs) and antibiotics. Here, we report the extremely promising anti-biofilm and immunomodulatory activities of human HDP GVF27 on two of the most clinically relevant Bcc members, as Burkholderia multivorans and Burkholderia cenocepacia. The effects of synthetic and labelled GVF27 were tested on B. cenocepacia and B. multivorans biofilms, at three different stages of formation, by alternative microscopy approaches. Assays on bacterial cultures and on human monocytes challenged with B. cenocepacia LPS, were also performed. GVF27 exerts, at different stages of formation, meaningful anti-biofilm effects towards both Bcc strains, a significant propensity to function in combination with ciprofloxacin, a relevant affinity for LPSs isolated from Burkholderia cenocepacia as well as a good propensity to mitigate the release of pro-inflammatory cytokines in human cells pre-treated with the same endotoxin. Overall, all these findings contribute to the elucidation of the main features that a good therapeutic agent directed against these extremely leathery biofilm-forming bacteria should possess.
Published: 2021
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32. Rescue of a lysosomal storage disorder caused by Grn loss-of-function with a brain penetrant progranulin biologic

Author: Ryan J. Watts, Kathryn M. Monroe, Junhua Wang, Melina Lenser, Jennifer Hsiao-Nakamoto, Hoang Nguyen, Todd P. Logan, Do Jin Kim, Fen Huang, Ritesh Ravi, Gilbert Di Paolo, Anil Rana, Kannan Gunasekaran, Yaneth Robles-Colmenares, Gerald M. Cherf, Buyankhishig Tsogtbaatar, Ceyda Llapashtica, Kirk R. Henne, Hilda Solanoy, Pascal E. Sanchez, Yashas Rajendra, Mihalis Kariolis, Ray Lieh Yoon Low, Roni Chau, Laralynne Przybyla, Michelle E. Pizzo, Chi-Lu Chiu, Meng Fang, Anastasia G. Henry, Giuseppe Astarita, Mark S. Dennis, Adam L. Boxer, Sarah L. DeVos, Sonnet S. Davis, Hilary W. Heuer, René Meisner, Joseph W. Lewcock, Devendra B. Srivastava, Bradley F. Boeve, Meredith E. K. Calvert, Katrina W. Lexa, Rachel Prorok, Lukas L. Skuja, Dolores Diaz, Akhil Bhalla, Matthew Simon, Jung H. Suh, Ankita Srivastava, Timothy K. Earr, Howard J. Rosen, Joseph Duque, Bettina Van Lengerich, and Elizabeth W. Sun
Subjects: Male, Neurodegenerative, Inbred C57BL, medicine.disease_cause, Medical and Health Sciences, Transgenic, Mice, neurodegenerative disease, Progranulins, Immunologic, Receptors, 2.1 Biological and endogenous factors, Tissue Distribution, Gliosis, Aetiology, Receptors, Immunologic, lipofuscin, Alzheimer's Disease Related Dementias (ADRD), Membrane Glycoproteins, Microglia, Transferrin, Brain, Biological Sciences, metabolomics, Cell biology, Frontotemporal Dementia (FTD), medicine.anatomical_structure, Phenotype, Galectin-3, Frontotemporal Dementia, Neurological, Bone Morphogenetic Proteins, lysosome, GBA, Female, LBPA, Induced Pluripotent Stem Cells, Transferrin receptor, Mice, Transgenic, Endosomes, Biology, General Biochemistry, Genetics and Molecular Biology, Article, Lipofuscin, lipids, Rare Diseases, Lysosome, galectin-3, Receptors, Transferrin, Acquired Cognitive Impairment, medicine, Animals, Humans, Loss function, Inflammation, Biological Products, Macrophages, Neurosciences, Alzheimer's Disease including Alzheimer's Disease Related Dementias (AD/ADRD), Lipid Metabolism, Brain Disorders, Lysosomal Storage Diseases, Mice, Inbred C57BL, Nerve Degeneration, lipidomics, Dementia, lysobisphosphatidic acid, Lysosomes, Glucocerebrosidase, Oxidative stress, Developmental Biology
Abstract: GRN mutations cause frontotemporal dementia (GRN-FTD) due to deficiency in progranulin (PGRN), a lysosomal and secreted protein with unclear function. Here, we found that Grn(−/−) mice exhibit a global deficiency in bis(monoacylglycero)phosphate (BMP), an endolysosomal phospholipid we identified as a pH-dependent PGRN interactor as well as a redox-sensitive enhancer of lysosomal proteolysis and lipolysis. Grn(−/−) brains also showed an age-dependent, secondary storage of glucocerebrosidase substrate glucosylsphingosine. We investigated a protein replacement strategy by engineering protein transport vehicle (PTV):PGRN – a recombinant protein linking PGRN to a modified Fc domain that binds human transferrin receptor for enhanced CNS biodistribution. PTV:PGRN rescued various Grn(−/−) phenotypes in primary murine macrophages and human iPSC-derived microglia, including oxidative stress, lysosomal dysfunction and endomembrane damage. Peripherally delivered PTV:PGRN corrected levels of BMP, glucosylsphingosine and disease pathology in Grn(−/−) CNS, including microgliosis, lipofuscinosis and neuronal damage. PTV:PGRN thus represents a potential biotherapeutic for GRN-FTD.
Published: 2021

33. Safety of a feed additive consisting of a tincture derived from Verbascum thapsus L. (great mullein tincture) for use in all animal species (MANGHEBATI SAS)

Author: Birgit Dusemund, Efsa Panel on Additives, Fabiola Pizzo, Alena Pechová, Ruud Woutersen, Henrik Christensen, Baltasar Mayo, Yolanda Sanz, Giovanna Azimonti, Mariana Petkova, Vasileios Bampidis, Fernando Ramos, Johannes Westendorf, Secundino López Puente, Paul Brantom, Roberto Edoardo Villa, Marta López-Alonso, Maria de Lourdes Bastos, Maryline Kouba, Francesca Marcon, Paola Manini, Andrew Chesson, and Mojca Fašmon Durjava
Subjects: safety, Animal feed, Veterinary (miscellaneous), Feed additive, great mullein tincture, TP1-1185, Plant Science, Biology, Microbiology, flavouring compounds, Anim2953, chemistry.chemical_compound, TX341-641, Dry matter, Verbascum thapsus L, Animal nutrition, Aucubin, Traditional medicine, Nutrition. Foods and food supply, sensory additives, Chemical technology, aucubin, Tincture, biology.organism_classification, Scientific Opinion, chemistry, Polyphenol, Verbascum thapsus, Animal Science and Zoology, Parasitology, Food Science
Abstract: The tincture derived from Verbascum thapsus L. (great mullein tincture) is intended to be used as a sensory additive in feed for all animal species. The product is a water/ethanol solution, with a dry matter content of ˜ 2.8% and contains on average 0.216% polyphenols including 0.093% flavonoids. According to a previous assessment, the additive was not characterised in full and about 82% of the dry matter fraction remained uncharacterised (representing 2.26% of the tincture). There was also uncertainty on the potential presence of iridoid glycosides in the tincture. Therefore, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) could not conclude on the safety of the additive at the proposed use levels of up to 50 g/kg complete feed for all animal species or for the consumer. The applicant has provided new data which show that the unidentified fraction consists of crude fibre, other carbohydrates, and protein. The tincture also contains aucubin (0.004%). Considering the genotoxic potential of aucubin and other related iridoids, no conclusions can be drawn for long‐living animals (pets and other non‐food producing animals, horses and animals for reproduction). For short‐living animals (animals for fattening), the FEEDAP Panel concludes that the tincture is safe at the maximum proposed use level of 50 mg/kg complete feed and that the use in water for drinking is safe provided that the total daily intake of the additive does not exceed the daily amount that is considered safe when consumed via feed. No safety concerns would arise for the consumer from the use of the tincture up to the highest safe level in animal nutrition. In the absence of data, no conclusions can be drawn on the potential of the tincture to be a dermal/eye irritant or a skin sensitiser.
Published: 2021
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34. Safety and efficacy of a feed additive consisting of Saccharomyces cerevisiae MUCL 39885 (Biosprint®) for all pigs (other than sows and weaned piglets) and other minor porcine species (Prosol S.p.A.)

Author: Ruud Woutersen, Paola Manini, Marta López-Alonso, Efsa Panel on Additives, Elisa Pettenati, Baltasar Mayo, Vasileios Bampidis, Henrik Christensen, Fabiola Pizzo, Maria de Lourdes Bastos, Maryline Kouba, Mariana Petkova, Mojca Fašmon Durjava, Fernando Ramos, Birgit Dusemund, Jaume Galobart, Montserrat Anguita, Yolanda Sanz, Francesca Marcon, Alena Pechová, Roberto Edoardo Villa, Giovanna Azimonti, Secundino López Puente, and Jordi Tarrés-Call
Subjects: Veterinary (miscellaneous), Feed additive, animal diseases, Saccharomyces cerevisiae, Plant Science, TP1-1185, other minor porcine species, Microbiology, QPS, Anim2953, Porcine species, Animal science, Weaned piglets, TX341-641, renewal, biology, integumentary system, Nutrition. Foods and food supply, Chemical technology, pigs, biology.organism_classification, Scientific Opinion, zootechnical additive, Animal Science and Zoology, Parasitology, Biosprint, Food Science
Abstract: The additive Biosprint® contains viable cells of Saccharomyces cerevisiae MUCL 39885 and is authorised as a feed additive in sows, dairy cows, horses, piglets (weaned), cattle for fattening, minor ruminants for fattening and minor ruminants for dairy products. The applicant has requested to extend the use of the additive to all pigs (other than sows and weaned piglets) and other minor porcine species at a minimum inclusion level of 3 × 109 CFU/kg feed. S. cerevisiae is considered by EFSA to have qualified presumption of safety (QPS) status and consequently is considered safe for the target species, the consumers and the environment. The additive is considered as a potential skin and eye irritant and a skin and respiratory sensitiser. In previous evaluations, the FEEDAP Panel concluded that the additive is efficacious in sows and weaned piglets. In the current application, these conclusions are extrapolated to all pigs (other than sows and weaned piglets) and to other minor porcine species.
Published: 2021

35. Familial Alzheimer’s disease presenilin-2 mutants affect Ca2+ homeostasis and brain network excitability

Author: Nelly Redolfi, Paola Pizzo, Diana Pendin, Elisa Greotti, Alessandro Leparulo, Cristina Fasolato, Tullio Pozzan, Elena Scremin, Riccardo Filadi, Chiara Gomiero, Emy Basso, Luisa Galla, and Nicola Vajente
Subjects: Aging, Amyloid beta, Cell, Mutant, Presenilin, Alzheimer’s disease, Amyloid-beta, Brain network, Ca2+ probes, Calcium homeostasis, 03 medical and health sciences, 0302 clinical medicine, mental disorders, medicine, Amyloid precursor protein, Dementia, 030212 general & internal medicine, biology, Neurodegeneration, medicine.disease, medicine.anatomical_structure, biology.protein, Geriatrics and Gerontology, Age of onset, Neuroscience, 030217 neurology & neurosurgery
Abstract: Alzheimer's disease (AD) is the most frequent cause of dementia in the elderly. Few cases are familial (FAD), due to autosomal dominant mutations in presenilin-1 (PS1), presenilin-2 (PS2) or amyloid precursor protein (APP). The three proteins are involved in the generation of amyloid-beta (Aβ) peptides, providing genetic support to the hypothesis of Aβ pathogenicity. However, clinical trials focused on the Aβ pathway failed in their attempt to modify disease progression, suggesting the existence of additional pathogenic mechanisms. Ca2+ dysregulation is a feature of cerebral aging, with an increased frequency and anticipated age of onset in several forms of neurodegeneration, including AD. Interestingly, FAD-linked PS1 and PS2 mutants alter multiple key cellular pathways, including Ca2+ signaling. By generating novel tools for measuring Ca2+ in living cells, and combining different approaches, we showed that FAD-linked PS2 mutants significantly alter cell Ca2+ signaling and brain network activity, as summarized below.
Published: 2019
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36. Targeting cell surface GRP78 enhances pancreatic cancer radiosensitivity through YAP/TAZ protein signaling

Author: Udhayakumar Gopal, Yvonne M. Mowery, Salvatore V. Pizzo, and Kenneth Young
Subjects: Transcriptional Activation, 0301 basic medicine, Cell signaling, Cell, Tafazzin, Gene Expression, Radiation Tolerance, Biochemistry, 03 medical and health sciences, Cell Line, Tumor, Radioresistance, medicine, Humans, Endoplasmic Reticulum Chaperone BiP, Molecular Biology, Protein kinase B, Heat-Shock Proteins, Adaptor Proteins, Signal Transducing, Cell Proliferation, 030102 biochemistry & molecular biology, biology, Cell growth, Chemistry, Dose-Response Relationship, Radiation, YAP-Signaling Proteins, Molecular Bases of Disease, Cell Biology, Pancreatic Neoplasms, 030104 developmental biology, medicine.anatomical_structure, Cancer cell, biology.protein, Cancer research, DLC1, Acyltransferases, Carcinoma, Pancreatic Ductal, Transcription Factors
Abstract: Ionizing radiation (IR) can promote migration and invasion of cancer cells, but the basis for this phenomenon has not been fully elucidated. IR increases expression of glucose-regulated protein 78kDa (GRP78) on the surface of cancer cells (CS-GRP78), and this up-regulation is associated with more aggressive behavior, radioresistance, and recurrence of cancer. Here, using various biochemical and immunological methods, including flow cytometry, cell proliferation and migration assays, Rho activation and quantitative RT-PCR assays, we investigated the mechanism by which CS-GRP78 contributes to radioresistance in pancreatic ductal adenocarcinoma (PDAC) cells. We found that activated α(2)-Macroglobulin (α(2)M*) a ligand of the CS-GRP78 receptor, induces formation of the AKT kinase (AKT)/DLC1 Rho-GTPase-activating protein (DLC1) complex and thereby increases Rho activation. Further, CS-GRP78 activated the transcriptional coactivators Yes-associated protein (YAP) and tafazzin (TAZ) in a Rho-dependent manner, promoting motility and invasiveness of PDAC cells. We observed that radiation-induced CS-GRP78 stimulates the nuclear accumulation of YAP/TAZ and increases YAP/TAZ target gene expressions. Remarkably, targeting CS-GRP78 with C38 monoclonal antibody (Mab) enhanced radiosensitivity and increased the efficacy of radiation therapy by curtailing PDAC cell motility and invasion. These findings reveal that CS-GRP78 acts upstream of YAP/TAZ signaling and promote migration and radiation-resistance in PDAC cells. We therefore conclude that, C38 Mab is a promising candidate for use in combination with radiation therapy to manage PDAC.
Published: 2019
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37. Rare variants in the genetic background modulate cognitive and developmental phenotypes in individuals carrying disease-associated variants

Author: Ji-eun Yoon, Arjun Krishnan, Marie Vincent, Marco Fichera, Claire Beneteau, Erik A. Sistermans, Nathalie Marle, Luana Mandarà, Sau Wai Cheung, R. Frank Kooy, Teresa Mattina, Rachel L. Kember, Mathilde Nizon, Jill A. Rosenfeld, Alexandre Reymond, Bertrand Isidor, Sophie Blesson, Jean-Hubert Caberg, Cindy Skinner, Emanuela Avola, Charles Perrine, Paolo Prontera, Susan Zeesman, Małgorzata J.M. Nowaczyk, Kate Pope, Lucilla Pizzo, David J. Amor, Boris Keren, Matthew Jensen, Katrin Männik, Patrick Callier, Pawel Stankiewicz, Damian Pazuchanics, Els Voorhoeve, Ornella Galesi, Joris Andrieux, Lucia Castiglia, Anne Laure Mosca-Boidron, Mathilde Lefebvre, Charles E. Schwartz, Santhosh Girirajan, Elizabeth McCready, Anke Van Dijck, Sandra Mercier, Maja Bucan, Corrado Romano, Laurence Faivre, Francesca Mari, Dominique Martin-Coignard, Vijay Kumar, Alessandra Renieri, Andrew Polyak, Emily Huber, Cédric Le Caignec, Aurora Currò, Olivier Pichon, Pennsylvania State University (Penn State), Penn State System, Baylor College of Medicine (BCM), Baylor University, Center for Integrative Genomics - Institute of Bioinformatics, Génopode (CIG), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL)-Université de Lausanne (UNIL), Michigan State University [East Lansing], Michigan State University System, McMaster University [Hamilton, Ontario], Service de génétique médicale - Unité de génétique clinique [Nantes], Université de Nantes (UN)-Centre hospitalier universitaire de Nantes (CHU Nantes), Antwerp University Hospital [Edegem] (UZA), Murdoch Children's Research Institute (MCRI), Department of Clinical Genetics (Academic Medical Center, University of Amsterdam), VU University Medical Center [Amsterdam], Perelman School of Medicine, University of Pennsylvania [Philadelphia], Medical Genetics, Service de Génétique Médicale, Hôpital Bretonneau, Tours, Laboratoire de génétique médicale et cytogénétique [Le Mans], Centre Hospitalier Le Mans (CH Le Mans), Laboratoire de Génétique Chromosomique et Moléculaire [CHU Dijon], Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Centre Hospitalier Universitaire de Liège (CHU-Liège), Centre de génétique - Centre de référence des maladies rares, anomalies du développement et syndromes malformatifs (CHU de Dijon), Greenwood Genetic Center, CHU Pitié-Salpêtrière [AP-HP], Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Greenwood Genetic Center [Greenwood, South Carolina, USA], Institut de Génétique Médicale [CHRU Lille], Hôpital Jeanne de Flandre [Lille]-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Human genetics, Amsterdam Neuroscience - Complex Trait Genetics, and Amsterdam Reproduction & Development (AR&D)
Subjects: Male, Parents, 0301 basic medicine, Proband, Neuronal, Genetic Carrier Screening, 16p11.2 deletion, 030105 genetics & heredity, Cognition, Family history, Neural Cell Adhesion Molecules, Genetics (clinical), Exome sequencing, Sequence Deletion, Genetics, Phenotype, Penetrance, Pedigree, Autistic Disorder/genetics, Autistic Disorder/physiopathology, Cell Adhesion Molecules, Neuronal/genetics, Chromosomes, Human, Pair 16/genetics, Cognition/physiology, DNA Copy Number Variations/genetics, Female, Gene Expression Regulation/genetics, Genetic Background, Humans, Methyltransferases/genetics, Nerve Tissue Proteins/genetics, Proteins/genetics, Sequence Deletion/genetics, Siblings, CNV, autism, modifier, phenotypic variability, Human, DNA Copy Number Variations, Cell Adhesion Molecules, Neuronal, Nerve Tissue Proteins, Biology, Chromosomes, Article, 03 medical and health sciences, mental disorders, medicine, Autistic Disorder, Gene, Pair 16, Calcium-Binding Proteins, Proteins, Methyltransferases, medicine.disease, Cytoskeletal Proteins, 030104 developmental biology, Gene Expression Regulation, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, Autism, Human medicine, Chromosomes, Human, Pair 16, Cell Adhesion Molecules, Transcription Factors
Abstract: Purpose: To assess the contribution of rare variants in the genetic background toward variability of neurodevelopmental phenotypes in individuals with rare copy-number variants (CNVs) and gene-disruptive variants. Methods: We analyzed quantitative clinical information, exome sequencing, and microarray data from 757 probands and 233 parents and siblings who carry disease-associated variants. Results: The number of rare likely deleterious variants in functionally intolerant genes (“other hits”) correlated with expression of neurodevelopmental phenotypes in probands with 16p12.1 deletion (n=23, p=0.004) and in autism probands carrying gene-disruptive variants (n=184, p=0.03) compared with their carrier family members. Probands with 16p12.1 deletion and a strong family history presented more severe clinical features (p=0.04) and higher burden of other hits compared with those with mild/no family history (p=0.001). The number of other hits also correlated with severity of cognitive impairment in probands carrying pathogenic CNVs (n=53) or de novo pathogenic variants in disease genes (n=290), and negatively correlated with head size among 80 probands with 16p11.2 deletion. These co-occurring hits involved known disease-associated genes such as SETD5, AUTS2, and NRXN1, and were enriched for cellular and developmental processes. Conclusion: Accurate genetic diagnosis of complex disorders will require complete evaluation of the genetic background even after a candidate disease-associated variant is identified.
Published: 2019
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38. Dynamic mechanical analysis (DMA) at room temperature of archaeological wood treated with various consolidants

Author: Benedetto Pizzo, Nicola Macchioni, Elisa Pecoraro, and Antonella Salvini
Subjects: 040101 forestry, Softwood, Materials science, biology, technology, industry, and agriculture, Rosin, 04 agricultural and veterinary sciences, 02 engineering and technology, Dynamic mechanical analysis, Polyethylene, 021001 nanoscience & nanotechnology, biology.organism_classification, Equilibrium moisture content, Viscoelasticity, Abies alba, Biomaterials, chemistry.chemical_compound, chemistry, medicine, 0401 agriculture, forestry, and fisheries, Pinus pinaster, Composite material, 0210 nano-technology, Kauramin, lactitol, PEG, polyethylene- L-tartaramide, rosin, silanes, stiffness of treated wood, waterlogged archaeological wood, wood conservation, medicine.drug
Abstract: The viscoelastic properties of wood samples treated with various consolidants [polyethylene glycols (PEGs), lactitol and trehalose, Kauramin, polydimethylsiloxane (PDMS) and trimethoxymethylsilane (MTMS), rosin and polyethylene-L-tartaramide] were evaluated by means of dynamic mechanical analysis (DMA) in order to clarify their effects with regard to the conservation of wood objects. Two softwoods, medium-decayed silver fir (Abies alba) and highly decayed maritime pine (Pinus pinaster), and two differently decayed oak hardwoods (Quercus spp.) were used. In addition, the selected parameters [retention, volume variations and equilibrium moisture content (EMC)] were evaluated to assess the consolidation efficacy. The results showed that in treated wood, both the storage modulus and tanδ depend upon the level of degradation. The impact of the consolidating product was greater in more degraded wood (a higher product amount inside the artefact) compared to well-preserved material, where also wood played a role (also when the products were applied at high concentrations). The values of the different viscoelastic parameters also depend upon the ability of the products to interact with the wood matrix; this characteristic is fundamental to the nature of each consolidant. Lactitol-treated samples showed the highest stiffness increases, whereas those treated with selected PEG combinations and rosin displayed noticeable tanδ increases (high dissipative behaviour).
Published: 2019
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39. Psychometric properties of the Brazilian version of the Coach–Athlete Relationship Questionnaire for coaches

Author: Lenamar Fiorese, Sophia Jowett, Caio Rosas Moreira, Gislaine Contessoto Pizzo, Selso Ananias Sitoe, José Roberto Andrade do Nascimento Junior, and Andressa Ribeiro Contreira
Subjects: biology, Team sport, Athletes, education, 05 social sciences, Applied psychology, 030229 sport sciences, biology.organism_classification, Sport psychology, 050105 experimental psychology, 03 medical and health sciences, Interpersonal relationship, 0302 clinical medicine, 0501 psychology and cognitive sciences, Psychology, human activities, Social Sciences (miscellaneous)
Abstract: The aim of this study was to assess the psychometric properties of the Brazilian version of the Coach–Athlete Relationship Questionnaire (CART-Q) for coaches. Subjects were 173 coaches (20–65 years old) from both sexes, from individual and team sports, ranging from amateur to national level; the instruments were the Coach version of CART-Q translated and adapted to Portuguese and the Athletic Satisfaction Scale adapted for coaches. Data analysis consisted of confirmatory factor analysis, internal consistency (Cronbach's alpha and composite reliability), concurrent validity (Spearman correlation), and temporal stability (intraclass correlation coefficient, ICC). Confirmatory factor analysis revealed a model with 11 items presenting adequate fit (χ2/df = 2.68; comparative fit index = 0.92; goodness-of-fit index = 0.91; Tucker–Lewis index = 0.90; root mean square error of approximation = 0.10) and the existence of a second-order factor (coach–athlete relationship). The scale has shown satisfactory internal consistency (composite reliability > 0.70 and α > 0.70). Concurrent validity assessment presented significant relationships (r > 0.40) with all coach satisfaction variables and temporal stability after 15 days was also adequate (0.65
Published: 2019
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40. Safety and efficacy of a feed additive consisting of an essential oil from the fruits of Litsea cubeba (Lour.) Pers. (litsea berry oil) for use in all animal species (FEFANA asbl)

Author: Paola Manini, Yolanda Sanz, Maria de Lourdes Bastos, Birgit Dusemund, Maryline Kouba, Andrew Chesson, Mojca Fašmon Durjava, Paul Brantom, Baltasar Mayo, Fernando Ramos, Ruud Woutersen, Efsa Panel on Additives, Roberto Edoardo Villa, Henrik Christensen, Vasileios Bampidis, Francesca Marcon, Alena Pechová, Giovanna Azimonti, Secundino López Puente, Mariana Petkova, Fabiola Pizzo, Johannes Westendorf, and Marta López-Alonso
Subjects: Veterinary (miscellaneous), Feed additive, component‐based approach, TP1-1185, Plant Science, Berry, Biology, Microbiology, geranial, law.invention, flavouring compounds, Anim2953, Litsea cubeba (Lour.) Pers, law, TX341-641, Animal species, Essential oil, Litsea, Traditional medicine, Nutrition. Foods and food supply, sensory additives, Chemical technology, Litsea cubeba, biology.organism_classification, Scientific Opinion, neral, Animal Science and Zoology, Parasitology, litsea berry oil, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of an essential oil from the fruits of Litsea cubeba (Lour.) Pers. (litsea berry oil), when used as a sensory additive (flavouring) in feed and water for drinking for all animal species. The FEEDAP Panel concluded that litsea berry oil is safe up to the maximum proposed use level of 125 mg/kg complete feed for ornamental fish. For the other species, the calculated safe concentration in complete feed are 11 mg/kg for chicken for fattening, 16 mg/kg for laying hen, 14 mg/kg for turkey for fattening, 19 mg/kg for piglet, 23 mg/kg for pig for fattening, 28 mg/kg for lactating sow, 48 mg/kg for veal calf (milk replacer), 43 mg/kg for cattle for fattening, sheep, goat and horse, 28 mg/kg for dairy cow, 17 mg/kg for rabbit, 47 mg/kg for salmon, 50 mg/kg for dog and 8.5 mg/kg for cat. The FEEDAP Panel also concluded that the use of litsea berry oil at the maximum proposed use level in water for drinking of 1 mg/kg is safe for all animal species. Simultaneous use in feed and water for drinking may lead to the maximum safe dose being exceeded. No concerns for consumer safety were identified following the use of the additive up to the highest safe use level in feed for the target animals. The essential oil under assessment should be considered as irritant to skin and eyes, and as a skin and respiratory sensitiser. The use of the additive in animal feed under the proposed conditions was not expected to pose a risk for the environment. Litsea berry oil is recognised to flavour food. Since its function in feed would be essentially the same as that in food, no further demonstration of efficacy was considered necessary.
Published: 2021

41. Safety and efficacy of feed additives consisting of Vitamin B2 (98%) and Vitamin B2 (80%) as riboflavin produced by Bacillus subtilis KCCM 10445 for all animal species (Hubei Guangji Pharmaceutical Co. Ltd.)

Author: Yolanda Sanz, Birgit Dusemund, Henrik Christensen, Elisa Pettenati, Giovanna Azimonti, Baltasar Mayo, Roberto Edoardo Villa, Montserrat Anguita, Joana Revez, Secundino López Puente, Vasileios Bampidis, Alena Pechová, Paola Manini, Jürgen Gropp, Fernando Ramos, Efsa Panel on Additives, Mojca Fašmon Durjava, Jaume Galobart, Jordi Tarrés-Call, Francesca Marcon, Marta López-Alonso, Mariana Petkova, Fabiola Pizzo, Ruud Woutersen, Maria de Lourdes Bastos, and Maryline Kouba
Subjects: safety, biology, Chemistry, Nutrition. Foods and food supply, Veterinary (miscellaneous), Chemical technology, efficacy, nutritional additive, Riboflavin, Plant Science, Bacillus subtilis, TP1-1185, biology.organism_classification, vitamins, Microbiology, Animal Science and Zoology, Parasitology, TX341-641, Food science, Animal species, Vitamin B2/Riboflavin, Food Science, Vitamin b2
Abstract: Following a request from the European Commission, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of vitamin B2 98% and vitamin B2 80% in the form of riboflavin produced by fermentation with a genetically modified strain of Bacillus subtilis (KCCM 10445) as nutritional additives in feed and water for drinking for all animal species. The production strain harbours antimicrobial resistance genes. With the data available the Panel is not in the position to confirm the correspondence between the strain deposited under accession number KCCM 10445 and the strain under the current assessment. The production strain and its recombinant DNA were not detected in the final products. Therefore, the additives do not pose any safety concern associated with the genetic modification of the production strain. The additives are safe for the target species, the consumer and the environment. Vitamin B2 80% is not hazardous by inhalation. In the absence of data, no conclusions on the possible risk by inhalation of vitamin B2 98% can be reached. Neither vitamin B2 98% nor vitamin B2 80% are irritant to skin or eyes. In the absence of data, no conclusions on the skin sensitisation potential of the additives can be reached. The additives under assessment are effective in covering the animals’ requirements for vitamin B2 when administered via feed and/or water for drinking.
Published: 2021

42. Safety and efficacy of a feed additive consisting of expressed mandarin oil from the fruit peels of Citrus reticulata Blanco for use in all animal species (FEFANA asbl)

Author: Paola Manini, Mojca Fašmon Durjava, Henrik Christensen, Mariana Petkova, Paul Brantom, Francesca Marcon, Johannes Westendorf, Baltasar Mayo, Roberto Edoardo Villa, Marta López-Alonso, Alena Pechová, Birgit Dusemund, Vasileios Bampidis, Efsa Panel on Additives, Andrew Chesson, Fabiola Pizzo, Maria de Lourdes Bastos, Maryline Kouba, Yolanda Sanz, Secundino López Puente, Giovanna Azimonti, Ruud Woutersen, and Fernando Ramos
Subjects: Veterinary (miscellaneous), Feed additive, TP1-1185, Plant Science, Biology, Microbiology, flavouring compounds, Anim2953, chemistry.chemical_compound, d‐limonene, perillaldehyde, TX341-641, Food science, Animal species, Citrus reticulata Blanco, D limonene, Nutrition. Foods and food supply, sensory additives, Chemical technology, expressed mandarin oil, Perillaldehyde, Mandarin Oil, Scientific Opinion, chemistry, polymethoxylated flavones, Animal Science and Zoology, Parasitology, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of expressed mandarin oil from the fruit peels of Citrus reticulata Blanco, when used as a sensory additive (flavouring) in feed and water for drinking for all animal species. The FEEDAP Panel concluded that the essential oil under assessment is safe up to the maximum proposed use levels in complete feed of 15 mg/kg for poultry, 33 mg/kg for pigs, 30 mg/kg for ruminants, 40 mg/kg for horse, and 15 mg/kg for salmon and rabbit. The presence of perillaldehyde was identified as a source of potential concern. However, in target species fed citrus by‐products as part of daily feed the use of the expressed mandarin oil in feed was not expected to increase the exposure to perillaldehyde to a relevant extent (< 4%). For companion animals and ornamental fish not normally exposed to citrus by‐products, no conclusion can be drawn. The FEEDAP Panel considered that the use in water for drinking is safe provided that the total daily intake of the additive does not exceed the daily amount that is considered safe when consumed via feed. No concerns for consumer safety were identified following the use of the additive up to the maximum proposed use level in feed. The essential oil under assessment should be considered as irritant to skin, eyes and the respiratory tract, and as a skin sensitiser. The use of the additive in animal feed under the proposed conditions of use was not expected to pose a risk for the environment. Expressed mandarin oil was recognised to flavour food. Since its function in feed would be essentially the same as that in food, no further demonstration of efficacy was considered necessary.
Published: 2021
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43. Assessment of a feed additive consisting of RRR-alpha-tocopheryl acetate (vitamin E) for all animal species for the renewal of its authorisation (Specialty Ingredients (Europe) B.V. and Vitae Caps S.A.)

Author: Birgit Dusemund, Georges Bories, Jürgen Gropp, Fernando Ramos, Ruud Woutersen, Montserrat Anguita, Maria Vittoria Vettori, Alena Pechová, Henrik Christensen, Roberto Edoardo Villa, Jaume Galobart, Giovanna Azimonti, Mojca Fašmon Durjava, Efsa Panel on Additives, Secundino López Puente, Paola Manini, Elisa Pettenati, Jordi Tarrés-Call, Yolanda Sanz, Baltasar Mayo, Vasileios Bampidis, Francesca Marcon, Mariana Petkova, Fabiola Pizzo, Orsolya Holczknecht, Marta López-Alonso, Maria de Lourdes Bastos, and Maryline Kouba
Subjects: safety, Veterinary (miscellaneous), Feed additive, medicine.medical_treatment, Alpha (ethology), TP1-1185, Plant Science, vitamin E, Biology, Microbiology, chemistry.chemical_compound, medicine, TX341-641, Food science, Animal species, vitamins and pro‐vitamins, renewal, Nutrition. Foods and food supply, Chemical technology, Vitamin E, feed, Authorization, RRR‐alpha tocopheryl acetate, nutritional additive, Scientific Opinion, chemistry, Animal Science and Zoology, Parasitology, Tocopheryl acetate, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the assessment of the application for renewal of authorisation of RRR‐alpha‐tocopheryl acetate (vitamin E) as a feed additive for all animal species. The applicant provided data demonstrating that the additive currently in the market complies with the conditions of authorisation. The FEEDAP Panel confirms that the use of RRR‐alpha‐tocopheryl acetate under the current authorised conditions of use is safe for the target species, the consumers and the environment. No concern for user safety is expected from the use of the active substance; however, due to the lack of information, the FEEDAP Panel is not able to conclude on its skin sensitisation potential. To draw conclusions on the safety for the user of the final formulated additives, specific studies would be required. There is no need to assess the efficacy of RRR‐alpha‐tocopheryl acetate in the context of the renewal of the authorisation.
Published: 2021

44. Fatal cytokine release syndrome by an aberrant FLIP/STAT3 axis

Author: Manuela Iezzi, Katia Donadello, Zheng-Li Shi, Stefano Ugel, Stefania Canè, Ying Chen, Marco Chilosi, Ido Amit, Peter J. Murray, Vincenzo Bronte, Francesca Hofer, Enrico Polati, Evelina Tacconelli, Piera Amelia Iezzi, Andrea Capece, Francesco De Sanctis, Alessandra Fiore, Francesco Domenico Del Pizzo, Leonardo Gottin, Serena Zilio, Silvio Bicciato, Chiara Musiu, Simone Caligola, Roza Maria Barouni, Alessia Lamolinara, Domenico Angelucci, Ildo Polidoro, Paolo Serafini, Cristina Frusteri, Andrea Grilli, Annalisa Adamo, and Domenico Girelli
Subjects: Male, medicine.medical_treatment, C-FLIP, Inbred C57BL, Mice, 80 and over, Medicine, FLICE-INHIBITORY PROTEINS, STAT3, Aged, 80 and over, Caspase 8, biology, DEATH, Middle Aged, Pathophysiology, APOPTOSIS, Cytokine release syndrome, Cytokine, Cytokines, Female, medicine.symptom, Cytokine Release Syndrome, Signal Transduction, EXPRESSION, STAT3 Transcription Factor, Inflammation, Lung injury, Article, Immune system, Animals, Humans, Interleukin 6, Molecular Biology, Aged, TRANSPLANTATION, business.industry, SARS-CoV-2, FLICE-INHIBITORY PROTEINS, C-FLIP, NUCLEAR-LOCALIZATION, APOPTOSIS, INFLAMMATION, MACROPHAGE, EXPRESSION, COVID-19, DEATH, TRANSPLANTATION, NUCLEAR-LOCALIZATION, COVID-19, Cell Biology, medicine.disease, Mice, Inbred C57BL, Flip, Immunology, biology.protein, MACROPHAGE, business
Abstract: Inflammatory responses rapidly detect pathogen invasion and mount a regulated reaction. However, dysregulated anti-pathogen immune responses can provoke life-threatening inflammatory pathologies collectively known as cytokine release syndrome (CRS), exemplified by key clinical phenotypes unearthed during the SARS-Cov-2 pandemic. The underlying pathophysiology of CRS remains elusive. We found that FLIP, a protein that controls caspase-8 death pathways, was highly expressed in myeloid cells of COVID-19 lungs. FLIP controlled CRS by fueling a STAT3-dependent inflammatory program. Indeed, constitutive expression of a viral FLIP homologue in myeloid cells triggered a STAT3-linked, progressive and fatal inflammatory syndrome in mice, characterized by elevated cytokine output, lymphopenia, lung injury and multiple organ dysfunctions that mimicked human CRS. As STAT3-targeting approaches relieved inflammation, immune disorders, and organ failures in these mice, targeted intervention towards this pathway could suppress the lethal CRS inflammatory state.One sentence summaryFLIP-expressing myeloid cells are key drivers of CRS through aberrant overexpression of STAT3 pathway. STAT3-targeting is effective in mitigating CRS like severe COVID-19.
Published: 2021

45. Assessment of a feed additive consisting of all‐rac‐alpha tocopheryl acetate (vitamin E) for all animal species for the renewal of its authorisation (EUROPE‐ASIA Import Export GmbH)

Author: Fabiola Pizzo, Orsolya Holczknecht, Marta López-Alonso, Mariana Petkova, Paola Manini, Montserrat Anguita, Maria de Lourdes Bastos, Maryline Kouba, Georges Bories, Giovanna Azimonti, Maria Vittoria Vettori, Roberto Edoardo Villa, Mojca Fašmon Durjava, Alena Pechová, Elisa Pettenati, Baltasar Mayo, Vasileios Bampidis, Efsa Panel on Additives, Secundino López Puente, Yolanda Sanz, Henrik Christensen, Ruud Woutersen, Francesca Marcon, Birgit Dusemund, Jaume Galobart, Jürgen Gropp, Fernando Ramos, and Jordi Tarrés-Call
Subjects: safety, Veterinary (miscellaneous), Feed additive, medicine.medical_treatment, Alpha (ethology), Plant Science, vitamin E, TP1-1185, Biology, Microbiology, Anim2953, chemistry.chemical_compound, medicine, TX341-641, Food science, Animal species, vitamins and pro‐vitamins, renewal, Nutrition. Foods and food supply, Vitamin E, Chemical technology, feed, Authorization, nutritional additive, Scientific Opinion, chemistry, all‐rac-alpha tocopheryl acetate, Animal Science and Zoology, Parasitology, Tocopheryl acetate, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the assessment of the application for renewal of authorisation of all‐rac‐alpha tocopheryl acetate (vitamin E) as a feed additive for all animal species. The applicant provided data demonstrating that the additive currently in the market complies with the conditions of authorisation. The FEEDAP Panel confirms that the use of all‐rac‐alpha‐tocopheryl acetate under the current authorised conditions of use is safe for the target species, the consumers and the environment. No concern for user safety is expected from the use of the active substance; however, due to the lack of information, the FEEDAP Panel is not able to conclude on its skin sensitisation potential. To draw conclusions on the safety for the user of the final formulated additives, specific studies would be required. There is no need to assess the efficacy of all‐rac‐alpha‐tocopheryl acetate in the context of the renewal of the authorisation.
Published: 2021

46. Safety and efficacy of feed additives consisting of expressed lemon oil and its fractions from Citrus limon (L.) Osbeck and of lime oil from Citrus aurantiifolia (Christm.) Swingle for use in all animal species (FEFANA asbl)

Author: Maria de Lourdes Bastos, Ruud Woutersen, Fernando Ramos, Giovanna Azimonti, Maryline Kouba, Mojca Fašmon Durjava, Alena Pechová, Baltasar Mayo, Andrew Chesson, Henrik Christensen, Yolanda Sanz, Secundino López Puente, Efsa Panel on Additives, Mariana Petkova, Birgit Dusemund, Paul Brantom, Paola Manini, Roberto Edoardo Villa, Francesca Marcon, Vasileios Bampidis, Jaume Galobart, Fabiola Pizzo, Johannes Westendorf, and Marta López-Alonso
Subjects: Veterinary (miscellaneous), TP1-1185, Plant Science, Biology, engineering.material, Microbiology, flavouring compounds, chemistry.chemical_compound, perillaldehyde, furocoumarins, TX341-641, Animal species, Lime, Citrus limon (L.) Osbeck, Citrus limon, sensory additives, Nutrition. Foods and food supply, Chemical technology, Citrus aurantiifolia (Christm.) Swingle, Lemon oil, Perillaldehyde, Furocoumarins, Horticulture, chemistry, engineering, Animal Science and Zoology, Parasitology, Citrus aurantiifolia, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of expressed lemon oil and distilled lemon oil from Citrus limon (L.) Osbeck and lime oil from Citrus aurantiifolia (Christm.) Swingle, when used as sensory additives in feed for all animal species. The use of the expressed lemon oil and its residual fraction and the use of lime oil in feed is not expected to increase the exposure to furocoumarins and methoxycoumarins and perillaldehyde of those target species that are already fed citrus by‐products a relevant extent (< 10%). For companion animals and ornamental fish not normally exposed to citrus by‐products, no conclusion can be drawn. For the other species and for the distilled fraction of expressed lemon oil, the FEEDAP Panel concludes that the additives under assessment are safe at the maximum proposed or at reduced use levels in complete feed. The Panel considers that the use in water for drinking is safe provided that the total daily intake of the additive does not exceed the daily amount that is considered safe when consumed via feed. No concerns for consumer safety were identified following the use of the additives at the maximum proposed use level in feed. The additives under assessment should be considered as irritants to skin and eyes and the respiratory tract and as skin sensitisers. Since expressed lemon oil and its fractions contain furocoumarins, they may cause phototoxicity. The use of the additives under the proposed conditions of use in animal feed is not expected to pose a risk for the environment. Since C. limon and C. aurantiifolia and their preparations are recognised to flavour food and its function in feed would be essentially the same as that in food, no further demonstration of efficacy is considered necessary.
Published: 2021
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47. Safety and efficacy of a feed additive consisting of a preparation of benzoic acid, calcium formate and fumaric acid (AviMatrix® Z) for all avian species other than laying birds (Novus Europe S.A. / N.V)

Author: Fabiola Pizzo, Secundino López Puente, Baltasar Mayo, Ruud Woutersen, Birgit Dusemund, Orsolya Holczknecht, Vasileios Bampidis, Jaume Galobart, Yolanda Sanz, Marta López-Alonso, Elisa Pettenati, Jordi Tarrés-Call, Mojca Fašmon Durjava, Maria de Lourdes Bastos, Francesca Marcon, Mariana Petkova, Maryline Kouba, Giovanna Azimonti, Montserrat Anguita, Alena Pechová, Fernando Ramos, Paola Manini, Roberto Edoardo Villa, Efsa Panel on Additives, and Henrik Christensen
Subjects: safety, feed additive, Fumaric acid, 040301 veterinary sciences, Veterinary (miscellaneous), Feed additive, efficacy, avian species, TP1-1185, Plant Science, 010501 environmental sciences, Biology, 01 natural sciences, Microbiology, Anim2953, 0403 veterinary science, chemistry.chemical_compound, Animal science, TX341-641, zootechnical, 0105 earth and related environmental sciences, Benzoic acid, Nutrition. Foods and food supply, Chemical technology, AviMatrix®, 04 agricultural and veterinary sciences, Calcium formate, Scientific Opinion, chemistry, Margin of safety, Animal Science and Zoology, Parasitology, Food Science
Abstract: The additive AviMatrix® Z is a preparation of benzoic acid, calcium formate and fumaric acid and is authorised as a feed additive in chickens for fattening and reared for laying. The applicant has requested to extend the use of the additive to all avian species other than laying birds at a concentration range from 500 to 1,000 mg/kg of complete feed. The safety of the additive was previously assessed by the FEEDAP Panel that concluded that there were no concerns for the consumers and no risks for the environment. Given the particle size distribution and low dusting potential of the additive, the exposure of workers by inhalation and the subsequent health risks were expected to be low. AviMatrix® Z is not considered to be a skin/eye irritant or a skin sensitiser. The FEEDAP Panel is not aware of any new information that would lead to reconsider the conclusions drawn previously. The results of a new tolerance study showed that the additive is tolerated by turkeys for fattening at threefold the highest recommended dose (1,000 mg/kg feed). Therefore, the FEEDAP Panel concluded that the additive is safe for turkeys for fattening at the maximum recommended dose and this conclusion was extended to turkeys reared for breeding. Due to the absence of a margin of safety in a trial in chickens for fattening previously evaluated, the FEEDAP Panel could not extrapolate this conclusion to all other avian species up to the point of lay. The FEEDAP Panel concluded that the additive has the potential to be efficacious in all avian species other than laying and breeding birds.
Published: 2021
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48. Safety and efficacy of a feed additive consisting of a dried extract from the leaves of Ginkgo biloba L. (G. biloba dry extract) for use in cats and dogs (C.I.A.M.)

Author: Johannes Westendorf, Secundino López Puente, Francesca Marcon, Paola Manini, Marta López-Alonso, Yolanda Sanz, Paul Brantom, Andrew Chesson, Fabiola Pizzo, Baltasar Mayo, Ruud Woutersen, Mojca Fašmon Durjava, Roberto Edoardo Villa, Giovanna Azimonti, Mariana Petkova, Efsa Panel on Additives, Fernando Ramos, Birgit Dusemund, Henrik Christensen, Alena Pechová, Maria de Lourdes Bastos, Maryline Kouba, and Vasileios Bampidis
Subjects: safety, CATS, Traditional medicine, biology, Nutrition. Foods and food supply, Chemistry, Ginkgo biloba, sensory additives, Chemical technology, Veterinary (miscellaneous), Feed additive, efficacy, TP1-1185, Plant Science, biology.organism_classification, Microbiology, Anim2953, Scientific Opinion, Ginkgo biloba dry extract, flavonol glycoside, TX341-641, Animal Science and Zoology, Parasitology, Ginkgo biloba L, Food Science
Abstract: Following a request from the European Commission, the EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of a dried extract prepared from the leaves of Ginkgo biloba L. (G. biloba dry extract) when used as a sensory additive in feed for cats and dogs. G. biloba dry extract is specified to contain at least 24% flavonol glycosides, at least 6% terpene lactones and less than 5 ppm ginkgolic acids. Since uncertainty remains concerning the nature of up to 75% of the extract, the additive is not sufficiently characterised to allow an assessment based on the individual components. In view of the indication of potential carcinogenicity from the results of studies by the National Toxicology Program of the USA, obtained with a G. biloba extract comparable with the additive under assessment, the FEEDAP Panel concludes that the additive cannot be considered safe for cats and dogs. In the absence of data, no conclusions can be drawn on the safety for the user. In the absence of evidence that the extract acts as a flavour in animal feed or has an effect on palatability, the FEEDAP Panel was unable to conclude on the efficacy of the additive.
Published: 2021

49. High-resolution analysis of the human retina miRNome reveals isomiR variations and novel microRNAs

Author: Diego Carrella, Concetta Ambrosio, Marianthi Karali, Maria Persico, Vincenzo Nigro, Annamaria Carissimo, Veer Singh Marwah, Sandro Banfi, Michele Pinelli, Diego Ponzin, Mariateresa Pizzo, Diego di Bernardo, Stefano Ferrari, Margherita Mutarelli, Karali, Marianthi, Persico, Maria, Mutarelli, Margherita, Carissimo, Annamaria, Pizzo, Mariateresa, Singh Marwah, Veer, Ambrosio, Concetta, Pinelli, Michele, Carrella, Diego, Ferrari, Stefano, Ponzin, Diego, Nigro, Vincenzo, DI BERNARDO, Diego, Banfi, Sandro, Karali, M, Persico, M, Mutarelli, M, Carissimo, A, Pizzo, M, Marwah, V, Ambrosio, C, Pinelli, M, Carrella, D, Ferrari, S, Ponzin, D, and Di Bernardo, D
Subjects: 0301 basic medicine, MOUSE RETINA, ANIMAL DEVELOPMENT, SMALL RNAS, EXPRESSION, DIFFERENTIATION, CLUSTER, IMPACT, GENES, INACTIVATION, DEGENERATION, Retina homeostasis, Data Resources and Analyses, Retinal Pigment Epithelium, Computational biology, Biology, Bioinformatics, Retina, Deep sequencing, Transcriptome, 03 medical and health sciences, 0302 clinical medicine, IsomiR, microRNA, Genetics, medicine, Humans, Retinal pigment epithelium, High-Throughput Nucleotide Sequencing, eye diseases, MicroRNAs, 030104 developmental biology, medicine.anatomical_structure, sense organs, 030217 neurology & neurosurgery, Function (biology)
Abstract: MicroRNAs play a fundamental role in retinal development and function. To characterise the miRNome of the human retina, we carried out deep sequencing analysis on sixteen individuals. We established the catalogue of retina-expressed miRNAs, determined their relative abundance and found that a small number of miRNAs accounts for almost 90% of the retina miRNome. We discovered more than 3000 miRNA variants (isomiRs), encompassing a wide range of sequence variations, which include seed modifications that are predicted to have an impact on miRNA action. We demonstrated that a seed-modifying isomiR of the retina-enriched miR-124-3p was endowed with different targeting properties with respect to the corresponding canonical form. Moreover, we identified 51 putative novel, retina-specific miRNAs and experimentally validated the expression for nine of them. Finally, a parallel analysis of the human Retinal Pigment Epithelium (RPE)/choroid, two tissues that are known to be crucial for retina homeostasis, yielded notably distinct miRNA enrichment patterns compared to the retina. The generated data are accessible through an ad hoc database. This study is the first to reveal the complexity of the human retina miRNome at nucleotide resolution and constitutes a unique resource to assess the contribution of miRNAs to the pathophysiology of the human retina.
Published: 2016
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50. Combinatorial patterns of gene expression changes contribute to variable expressivity of the developmental delay-associated 16p12.1 deletion

Author: Arjun Krishnan, Santhosh Girirajan, Lucilla Pizzo, Maitreya Das, Anastasia Tyryshkina, Emily Huber, Matthew Jensen, and Corrine Smolen
Subjects: Ankyrins, Complex disorders, Gene regulatory network, Gene Expression, QH426-470, Biology, Transcriptome, Exome Sequencing, Gene expression, Genetics, Humans, Family, Copy-number variation, ANK3, Autistic Disorder, Copy-number variant, Molecular Biology, Gene, Genetics (clinical), Zinc Finger E-box Binding Homeobox 2, Inherited variants, Whole-genome sequencing, Whole Genome Sequencing, Research, Developmental disorders, Alternative splicing, Brain, Forkhead Transcription Factors, RNA sequencing, FOXP1, Phenotype, Human genetics, Phosphoric Monoester Hydrolases, Repressor Proteins, Biological Variation, Population, Expression quantitative trait loci, Molecular Medicine, Medicine, Chromosome Deletion, Transcription Factors
Abstract: Background Recent studies have suggested that individual variants do not sufficiently explain the variable expressivity of phenotypes observed in complex disorders. For example, the 16p12.1 deletion is associated with developmental delay and neuropsychiatric features in affected individuals, but is inherited in > 90% of cases from a mildly-affected parent. While children with the deletion are more likely to carry additional “second-hit” variants than their parents, the mechanisms for how these variants contribute to phenotypic variability are unknown. Methods We performed detailed clinical assessments, whole-genome sequencing, and RNA sequencing of lymphoblastoid cell lines for 32 individuals in five large families with multiple members carrying the 16p12.1 deletion. We identified contributions of the 16p12.1 deletion and “second-hit” variants towards a range of expression changes in deletion carriers and their family members, including differential expression, outlier expression, alternative splicing, allele-specific expression, and expression quantitative trait loci analyses. Results We found that the deletion dysregulates multiple autism and brain development genes such as FOXP1, ANK3, and MEF2. Carrier children also showed an average of 5323 gene expression changes compared with one or both parents, which matched with 33/39 observed developmental phenotypes. We identified significant enrichments for 13/25 classes of “second-hit” variants in genes with expression changes, where 4/25 variant classes were only enriched when inherited from the noncarrier parent, including loss-of-function SNVs and large duplications. In 11 instances, including for ZEB2 and SYNJ1, gene expression was synergistically altered by both the deletion and inherited “second-hits” in carrier children. Finally, brain-specific interaction network analysis showed strong connectivity between genes carrying “second-hits” and genes with transcriptome alterations in deletion carriers. Conclusions Our results suggest a potential mechanism for how “second-hit” variants modulate expressivity of complex disorders such as the 16p12.1 deletion through transcriptomic perturbation of gene networks important for early development. Our work further shows that family-based assessments of transcriptome data are highly relevant towards understanding the genetic mechanisms associated with complex disorders.
Published: 2021
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